Prodić, Ivana

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Authority KeyName Variants
orcid::0000-0003-0604-9246
  • Prodić, Ivana (29)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718. Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200042 (University of Belgrade, Institute of Molecular Genetics and Genetic Engineering)
Belgian Special Research Fund BOF StG No. 01 N01718 COST Action [FA 1005]
Ghent University Global Campus (GUGC), Incheon, Republic of Korea Serbian Academy of Sciences and Arts (grant number F-26)
Serbian Academy of Sciences and Arts Project F-26. Belgian Special Research Fund BOF StG [01N01718]
Belgian Special Research Fund BOF StG No. 01N01718 Belgian Special Research Fund BOF StG No. 01N01718.
COST Action [FA1005] Hesselman Foundation
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM) Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200032 (Institute of Field and Vegetable Crops, Novi Sad)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200134 (University of Novi Sad, Faculty of Technology) Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200177 (Immunology Research Centre 'Branislav Janković' Torlak, Belgrade)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200288 (Innovation Center of the Faculty of Chemistry) LEAPSyn-SCI - Late Embryogenesis Abundant Proteins: Structural Characterisation and Interaction With Α-Synuclein
King Gustaf V's 80-year Foundation Konsul Th C Bergh Foundation
Serbian Academy of Sciences and Arts GA No. F-26 Serbian Academy of Sciences and Arts GA No. F-26.
Stockholm County Council (ALF project)Stockholm County Council Swedish Asthma and Allergy Association's Research Foundation
Swedish Cancer and Allergy Foundation Swedish Heart-Lung FoundationSwedish Heart-Lung Foundation

Author's Bibliography

Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts

Smiljanić, Katarina; Prodić, Ivana; Trifunovic, Sara; Krstić Ristivojević, Maja; Aćimović, Milica; Stanković Jeremić, Jovana; Lončar, Biljana; Tešević, Vele

(MDPI, 2023)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Trifunovic, Sara
AU  - Krstić Ristivojević, Maja
AU  - Aćimović, Milica
AU  - Stanković Jeremić, Jovana
AU  - Lončar, Biljana
AU  - Tešević, Vele
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/857
AB  - As byproducts of essential oil distillation, hydrolates are used in natural cosmetics/biomedicine due to their beneficial skin effects. However, data on their safety with relevant biological targets, such as human skin cells, are scarce. Therefore, we have tested nine hydrolates from the Lamiaceae family with skin fibroblasts that are responsible for extracellular collagenous matrix builds. Thyme, oregano, and winter savoury hydrolates showed several times higher total phenolics, which correlated strongly with their radical scavenging and antioxidative capacity; there was no correlation between their viability profiles and the reducing sugar levels. No proteins/peptides were detected. All hydrolates appeared safe for prolonged skin exposure except for 10-fold diluted lavender, which showed cytotoxicity (~20%), as well as rosemary and lavandin (~10%) using viability, DNA synthesis, and cell count testing. Clary sage, oregano, lemon balm, and thyme hydrolates (10-fold diluted) increased fibroblast viability and/or proliferation by 10–30% compared with the control, while their viability remained unaffected by Mentha and winter savoury. In line with the STITCH database, increased viability could be attributed to thymol presence in oregano and thyme hydrolates in lemon balm, which is most likely attributable to neral and geranial. The proliferative effect of clary sage could be supported by alpha-terpineol, not linalool. The major volatile organic compounds (VOCs) associated with cytotoxic effects on fibroblasts were borneol, 1,8-cineole, and terpinene-4-ol. Further research with pure compounds is warranted to confirm the roles of VOCs in the observed effects that are relevant to cosmetic and wound healing aspects.
PB  - MDPI
T2  - Antioxidants
T2  - Antioxidants
T1  - Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts
IS  - 11
SP  - 1988
VL  - 12
DO  - 10.3390/antiox12111988
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Trifunovic, Sara and Krstić Ristivojević, Maja and Aćimović, Milica and Stanković Jeremić, Jovana and Lončar, Biljana and Tešević, Vele",
year = "2023",
abstract = "As byproducts of essential oil distillation, hydrolates are used in natural cosmetics/biomedicine due to their beneficial skin effects. However, data on their safety with relevant biological targets, such as human skin cells, are scarce. Therefore, we have tested nine hydrolates from the Lamiaceae family with skin fibroblasts that are responsible for extracellular collagenous matrix builds. Thyme, oregano, and winter savoury hydrolates showed several times higher total phenolics, which correlated strongly with their radical scavenging and antioxidative capacity; there was no correlation between their viability profiles and the reducing sugar levels. No proteins/peptides were detected. All hydrolates appeared safe for prolonged skin exposure except for 10-fold diluted lavender, which showed cytotoxicity (~20%), as well as rosemary and lavandin (~10%) using viability, DNA synthesis, and cell count testing. Clary sage, oregano, lemon balm, and thyme hydrolates (10-fold diluted) increased fibroblast viability and/or proliferation by 10–30% compared with the control, while their viability remained unaffected by Mentha and winter savoury. In line with the STITCH database, increased viability could be attributed to thymol presence in oregano and thyme hydrolates in lemon balm, which is most likely attributable to neral and geranial. The proliferative effect of clary sage could be supported by alpha-terpineol, not linalool. The major volatile organic compounds (VOCs) associated with cytotoxic effects on fibroblasts were borneol, 1,8-cineole, and terpinene-4-ol. Further research with pure compounds is warranted to confirm the roles of VOCs in the observed effects that are relevant to cosmetic and wound healing aspects.",
publisher = "MDPI",
journal = "Antioxidants, Antioxidants",
title = "Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts",
number = "11",
pages = "1988",
volume = "12",
doi = "10.3390/antiox12111988"
}
Smiljanić, K., Prodić, I., Trifunovic, S., Krstić Ristivojević, M., Aćimović, M., Stanković Jeremić, J., Lončar, B.,& Tešević, V.. (2023). Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts. in Antioxidants
MDPI., 12(11), 1988.
https://doi.org/10.3390/antiox12111988
Smiljanić K, Prodić I, Trifunovic S, Krstić Ristivojević M, Aćimović M, Stanković Jeremić J, Lončar B, Tešević V. Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts. in Antioxidants. 2023;12(11):1988.
doi:10.3390/antiox12111988 .
Smiljanić, Katarina, Prodić, Ivana, Trifunovic, Sara, Krstić Ristivojević, Maja, Aćimović, Milica, Stanković Jeremić, Jovana, Lončar, Biljana, Tešević, Vele, "Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts" in Antioxidants, 12, no. 11 (2023):1988,
https://doi.org/10.3390/antiox12111988 . .
2

Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica

Pantelić, Ana; Prodić, Ivana; Milić, Dejana; Senćanski, Milan; Vidović, Marija

(Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade, 2023)

TY  - CONF
AU  - Pantelić, Ana
AU  - Prodić, Ivana
AU  - Milić, Dejana
AU  - Senćanski, Milan
AU  - Vidović, Marija
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/824
AB  - Introduction: Resurrection plants (such as Ramonda serbica) can survive a long desiccation period andfully resume their metabolism upon watering. The hallmark of desiccation tolerance (DT) is the accumulation of protective, intrinsically disordered proteins(IDPs), called late embryogenesis abundant proteins (LEAPs). Although their high structural plasticity allows them to interact with various partners, nospecific cellular targets of LEAPs have been identified so far.Methods: To identify LEAPsinvolved in DT, differential transcriptome and proteome analyses of hydratedand desiccated R. serbica leaves were performed. The identified LEAPs were structurally characterisedand classified. To evaluate theirstructural propertiesin vitro and their potential functionsin vivo, the representative RsLEA proteins, were produced in Escherichia coli using recombinant DNA technology.Results: Members of the LEA4 protein family represent the majority of desiccation-inducible LEAPs. Even17 proteins belonging to the LEA4 protein family group were induced by desiccation. They show high disorder propensity (82 %), and at the same time, a high tendency to form α-helices (>80%). Although recombinant DNA technology has traditionally been used to overexpress and purify various globularproteins, the production of IDPsis challenging due to their high susceptibility to proteolytic cleavage andaggregation. Nevertheless, the representative LEAPs containing hexa-Histagsimmunoglobulin G-binding protein and a proteolytic TEV site were produced, purified and cleaved by TEV protease.Conclusion: The combination of in silico and in vitro results will be crucial for the identification of endogenous partners of LEAPs, providing further insight into their role in DT.
PB  - Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade
C3  - CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
T1  - Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica
EP  - 110
SP  - 110
UR  - https://hdl.handle.net/21.15107/rcub_intor_824
ER  - 
@conference{
author = "Pantelić, Ana and Prodić, Ivana and Milić, Dejana and Senćanski, Milan and Vidović, Marija",
year = "2023",
abstract = "Introduction: Resurrection plants (such as Ramonda serbica) can survive a long desiccation period andfully resume their metabolism upon watering. The hallmark of desiccation tolerance (DT) is the accumulation of protective, intrinsically disordered proteins(IDPs), called late embryogenesis abundant proteins (LEAPs). Although their high structural plasticity allows them to interact with various partners, nospecific cellular targets of LEAPs have been identified so far.Methods: To identify LEAPsinvolved in DT, differential transcriptome and proteome analyses of hydratedand desiccated R. serbica leaves were performed. The identified LEAPs were structurally characterisedand classified. To evaluate theirstructural propertiesin vitro and their potential functionsin vivo, the representative RsLEA proteins, were produced in Escherichia coli using recombinant DNA technology.Results: Members of the LEA4 protein family represent the majority of desiccation-inducible LEAPs. Even17 proteins belonging to the LEA4 protein family group were induced by desiccation. They show high disorder propensity (82 %), and at the same time, a high tendency to form α-helices (>80%). Although recombinant DNA technology has traditionally been used to overexpress and purify various globularproteins, the production of IDPsis challenging due to their high susceptibility to proteolytic cleavage andaggregation. Nevertheless, the representative LEAPs containing hexa-Histagsimmunoglobulin G-binding protein and a proteolytic TEV site were produced, purified and cleaved by TEV protease.Conclusion: The combination of in silico and in vitro results will be crucial for the identification of endogenous partners of LEAPs, providing further insight into their role in DT.",
publisher = "Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade",
journal = "CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia",
title = "Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica",
pages = "110-110",
url = "https://hdl.handle.net/21.15107/rcub_intor_824"
}
Pantelić, A., Prodić, I., Milić, D., Senćanski, M.,& Vidović, M.. (2023). Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade., 110-110.
https://hdl.handle.net/21.15107/rcub_intor_824
Pantelić A, Prodić I, Milić D, Senćanski M, Vidović M. Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia. 2023;:110-110.
https://hdl.handle.net/21.15107/rcub_intor_824 .
Pantelić, Ana, Prodić, Ivana, Milić, Dejana, Senćanski, Milan, Vidović, Marija, "Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica" in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia (2023):110-110,
https://hdl.handle.net/21.15107/rcub_intor_824 .

Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies

Prodić, Ivana; Krstić-Ristivojević, Maja; Smiljanić, Katarina

(MDPI, 2023)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Krstić-Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/756
AB  - Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.
PB  - MDPI
T2  - Antioxidants
T1  - Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies
IS  - 4
SP  - 886
VL  - 12
DO  - 10.3390/antiox12040886
ER  - 
@article{
author = "Prodić, Ivana and Krstić-Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.",
publisher = "MDPI",
journal = "Antioxidants",
title = "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies",
number = "4",
pages = "886",
volume = "12",
doi = "10.3390/antiox12040886"
}
Prodić, I., Krstić-Ristivojević, M.,& Smiljanić, K.. (2023). Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants
MDPI., 12(4), 886.
https://doi.org/10.3390/antiox12040886
Prodić I, Krstić-Ristivojević M, Smiljanić K. Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants. 2023;12(4):886.
doi:10.3390/antiox12040886 .
Prodić, Ivana, Krstić-Ristivojević, Maja, Smiljanić, Katarina, "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies" in Antioxidants, 12, no. 4 (2023):886,
https://doi.org/10.3390/antiox12040886 . .
1
3
3

Food allergies on the rise: the role of anthropogenic chemicals

Smiljanić, Katarina; Prodić, Ivana

(Udruženje za preventivnu pedijatriju Srbije, 2023)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/788
AB  - Food allergies have increased dramatically in the last decade, especially in developedcountries. Food tolerance requires strict maintenance of a specific microbial portfolio inthe gastrointestinal tract, as changes in the gut microbiome can lead to its disruption,which in turn causes inflammation and pathogenic gut conditions leading to thedevelopment of food allergies. Any environmental factors that lead to a disturbanceand/or malfunction of the gastrointestinal tract and digestive performance favor thedevelopment of food allergies.Based on that, what do we know about the role of increasing anthropogenic chemicals,including emerging ones, resulting from the new global situation?There is awareness that their effects are multifaceted, e.g., chemicals affect the growth ofplants and animals and thus the quality of the food produced. In addition, chemicals affectour food during its production and processing, but also affect our body andgastrointestinal tract. It is time to fill the knowledge gaps and understand how theseinteractions between environmental triggers such as industrial and traffic pollution,transition and heavy metals, pesticides, chemtrails, etc., affect food allergens and theirallergenicity, adjuvant effects, and the increasing prevalence of food allergies.Some improvements in this area are already being made through advances in ‘omics’technologies (i.e., proteomics, genomics, metabolomics) and systems biology approachesthat will hopefully provide a scientific understanding of the relationship betweenincreasing food allergies and the increasingly present wide variety of anthropogenicchemicals in our environment.
PB  - Udruženje za preventivnu pedijatriju Srbije
C3  - Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
T1  - Food allergies on the rise: the role of anthropogenic chemicals
EP  - 27
SP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_intor_788
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana",
year = "2023",
abstract = "Food allergies have increased dramatically in the last decade, especially in developedcountries. Food tolerance requires strict maintenance of a specific microbial portfolio inthe gastrointestinal tract, as changes in the gut microbiome can lead to its disruption,which in turn causes inflammation and pathogenic gut conditions leading to thedevelopment of food allergies. Any environmental factors that lead to a disturbanceand/or malfunction of the gastrointestinal tract and digestive performance favor thedevelopment of food allergies.Based on that, what do we know about the role of increasing anthropogenic chemicals,including emerging ones, resulting from the new global situation?There is awareness that their effects are multifaceted, e.g., chemicals affect the growth ofplants and animals and thus the quality of the food produced. In addition, chemicals affectour food during its production and processing, but also affect our body andgastrointestinal tract. It is time to fill the knowledge gaps and understand how theseinteractions between environmental triggers such as industrial and traffic pollution,transition and heavy metals, pesticides, chemtrails, etc., affect food allergens and theirallergenicity, adjuvant effects, and the increasing prevalence of food allergies.Some improvements in this area are already being made through advances in ‘omics’technologies (i.e., proteomics, genomics, metabolomics) and systems biology approachesthat will hopefully provide a scientific understanding of the relationship betweenincreasing food allergies and the increasingly present wide variety of anthropogenicchemicals in our environment.",
publisher = "Udruženje za preventivnu pedijatriju Srbije",
journal = "Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.",
title = "Food allergies on the rise: the role of anthropogenic chemicals",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_intor_788"
}
Smiljanić, K.,& Prodić, I.. (2023). Food allergies on the rise: the role of anthropogenic chemicals. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
Udruženje za preventivnu pedijatriju Srbije., 27-27.
https://hdl.handle.net/21.15107/rcub_intor_788
Smiljanić K, Prodić I. Food allergies on the rise: the role of anthropogenic chemicals. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.. 2023;:27-27.
https://hdl.handle.net/21.15107/rcub_intor_788 .
Smiljanić, Katarina, Prodić, Ivana, "Food allergies on the rise: the role of anthropogenic chemicals" in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023. (2023):27-27,
https://hdl.handle.net/21.15107/rcub_intor_788 .

Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix

Khulal, Urmila; Stojadinović, Marija M.; Prodić, Ivana; Rajković, Andrea; Ćirković-Veličković, Tanja

(Elsevier, 2023)

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/766
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
SP  - 134981
VL  - 405
DO  - 10.1016/j.foodchem.2022.134981
ER  - 
@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
pages = "134981",
volume = "405",
doi = "10.1016/j.foodchem.2022.134981"
}
Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981
Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .
Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .
2
4
3

Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix

Khulal, Urmila; Stojadinović, Marija M.; Prodić, Ivana; Rajković, Andrea; Ćirković-Veličković, Tanja

(Elsevier, 2023)

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/767
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
SP  - 134981
VL  - 405
UR  - https://hdl.handle.net/21.15107/rcub_intor_767
ER  - 
@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
pages = "134981",
volume = "405",
url = "https://hdl.handle.net/21.15107/rcub_intor_767"
}
Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://hdl.handle.net/21.15107/rcub_intor_767
Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
https://hdl.handle.net/21.15107/rcub_intor_767 .
Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://hdl.handle.net/21.15107/rcub_intor_767 .

Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart

Prodić, Ivana; Burazer, Lidija; Đorić, Nataša; Krstić-Ristivojević, Maja; Smiljanić, Katarina

(Udruženje za preventivnu pedijatriju Srbije, 2023)

TY  - CONF
AU  - Prodić, Ivana
AU  - Burazer, Lidija
AU  - Đorić, Nataša
AU  - Krstić-Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/771
AB  - Background and Aim: Epidemiological studies pointed at the connection betweenpollution (e.g., traffic emissions) and an increased percentage of people suffering fromrespiratory allergies, including the pediatric population. Field studies provided the mostrelevant assessment of the effects of the intensity and variety of urban and industrialcontamination on the structure and allergenic potency of pollen allergens. Therefore, theaim of the present work was to compare allergenic profiles ofDactylis glomerata pollen(DGP) collected in the specific urban and rural areas (Kruševac and suburbs), to assesspollen structures and immunoglobulin E (IgE) reactivity to pollen of school childrenpopulation allergic to grass pollens.
PB  - Udruženje za preventivnu pedijatriju Srbije
C3  - Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
T1  - Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart
EP  - 58
SP  - 58
UR  - https://hdl.handle.net/21.15107/rcub_intor_771
ER  - 
@conference{
author = "Prodić, Ivana and Burazer, Lidija and Đorić, Nataša and Krstić-Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Background and Aim: Epidemiological studies pointed at the connection betweenpollution (e.g., traffic emissions) and an increased percentage of people suffering fromrespiratory allergies, including the pediatric population. Field studies provided the mostrelevant assessment of the effects of the intensity and variety of urban and industrialcontamination on the structure and allergenic potency of pollen allergens. Therefore, theaim of the present work was to compare allergenic profiles ofDactylis glomerata pollen(DGP) collected in the specific urban and rural areas (Kruševac and suburbs), to assesspollen structures and immunoglobulin E (IgE) reactivity to pollen of school childrenpopulation allergic to grass pollens.",
publisher = "Udruženje za preventivnu pedijatriju Srbije",
journal = "Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.",
title = "Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart",
pages = "58-58",
url = "https://hdl.handle.net/21.15107/rcub_intor_771"
}
Prodić, I., Burazer, L., Đorić, N., Krstić-Ristivojević, M.,& Smiljanić, K.. (2023). Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
Udruženje za preventivnu pedijatriju Srbije., 58-58.
https://hdl.handle.net/21.15107/rcub_intor_771
Prodić I, Burazer L, Đorić N, Krstić-Ristivojević M, Smiljanić K. Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.. 2023;:58-58.
https://hdl.handle.net/21.15107/rcub_intor_771 .
Prodić, Ivana, Burazer, Lidija, Đorić, Nataša, Krstić-Ristivojević, Maja, Smiljanić, Katarina, "Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart" in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023. (2023):58-58,
https://hdl.handle.net/21.15107/rcub_intor_771 .

Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting

Smiljanić, Katarina; Prodić, Ivana; Đukić, Teodora; Vasović, Tamara; Jovanović, Vesna B.; Ćirković-Veličković, Tanja

(2021)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/780
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting
EP  - 71
SP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_intor_780
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_intor_780"
}
Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 71-71.
https://hdl.handle.net/21.15107/rcub_intor_780
Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_intor_780 .
Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):71-71,
https://hdl.handle.net/21.15107/rcub_intor_780 .

Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart

Prodić, Ivana; Smiljanić, Katarina; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(INFOGEST Cost action, INRAE, Teagasc LTD., 2021)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/755
AB  - Background: In vitro pepsin digestion is important factor when assessing protein foodallergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. Thereare only two studies employing in vitro INFOGEST digestion harmonized protocol onhazelnut with its full matrix. The aim of this study was to assess immunoreactivity of rawand roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9allergen purified from these two sources.Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, wereassessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structuralanalyses.Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yettheir large fragments survived partially. Cor a 8 was protected by lipids, retaining capabilityto bind its specific antibody. Roasting did not significantly affect secondary structure of themost abundant hazelnut allergen, Cor a 9.Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera ofhazelnut allergic patients with oral-gastric allergen digests.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart
EP  - 62
SP  - 62
UR  - https://hdl.handle.net/21.15107/rcub_intor_755
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: In vitro pepsin digestion is important factor when assessing protein foodallergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. Thereare only two studies employing in vitro INFOGEST digestion harmonized protocol onhazelnut with its full matrix. The aim of this study was to assess immunoreactivity of rawand roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9allergen purified from these two sources.Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, wereassessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structuralanalyses.Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yettheir large fragments survived partially. Cor a 8 was protected by lipids, retaining capabilityto bind its specific antibody. Roasting did not significantly affect secondary structure of themost abundant hazelnut allergen, Cor a 9.Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera ofhazelnut allergic patients with oral-gastric allergen digests.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart",
pages = "62-62",
url = "https://hdl.handle.net/21.15107/rcub_intor_755"
}
Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 62-62.
https://hdl.handle.net/21.15107/rcub_intor_755
Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:62-62.
https://hdl.handle.net/21.15107/rcub_intor_755 .
Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):62-62,
https://hdl.handle.net/21.15107/rcub_intor_755 .

Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol

Prodić, Ivana; Smiljanić, Katarina; Nagl, Christoph; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(Sociedade Portuguesa de Química, 2021)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/753
AB  - Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress
T1  - Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol
EP  - 126
SP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_intor_753
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress",
title = "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol",
pages = "126-126",
url = "https://hdl.handle.net/21.15107/rcub_intor_753"
}
Prodić, I., Smiljanić, K., Nagl, C., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress
Sociedade Portuguesa de Química., 126-126.
https://hdl.handle.net/21.15107/rcub_intor_753
Prodić I, Smiljanić K, Nagl C, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress. 2021;:126-126.
https://hdl.handle.net/21.15107/rcub_intor_753 .
Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol" in Book of Abstracts of the XXI EuroFoodChem Congress (2021):126-126,
https://hdl.handle.net/21.15107/rcub_intor_753 .

Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications

Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Đukić, Teodora; Vasović, Tamara; Jovanović, Vesna B.; Ćirković-Veličković, Tanja

(New York : Nova Science Publisher, 2020)

TY  - CHAP
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/764
AB  - Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.
PB  - New York : Nova Science Publisher
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications
SP  - 158
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_intor_764
ER  - 
@inbook{
author = "Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.",
publisher = "New York : Nova Science Publisher",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications",
pages = "158",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_intor_764"
}
Smiljanić, K., Mihailović, J., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2020). Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publisher., 4, 158.
https://hdl.handle.net/21.15107/rcub_intor_764
Smiljanić K, Mihailović J, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;4:158.
https://hdl.handle.net/21.15107/rcub_intor_764 .
Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 4 (2020):158,
https://hdl.handle.net/21.15107/rcub_intor_764 .

Food Allergens’ Susceptibility to Proteolysis

Prodić, Ivana; Smiljanić, Katarina; Radosavljević, Jelena

(New York : Nova Science Publishers, 2020)

TY  - CHAP
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Radosavljević, Jelena
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/765
AB  - Common properties of food allergens are prominent resistance to heat treatment and enzyme proteolysis. Stability of the proteins upon gastrointestinal proteolysis of food highly correlates with its allergenic potential. At this moment, the scientific community is putting a lot of effort to connect the available knowledge on the structure and function of food proteins, with stability to proteolysis in order to provide the most reliable prediction tool for allergenicity of novel proteins. Moreover, choosing the conditions under which gastrointestinal proteolysis is simulated may profoundly affect the results of assays and allergenicity assessment. At the beginning of research, for the link between allergenicity and proteolytic stability, purified allergens were used. However, this approchad was proved to be prone to production of erroneous data, since the proteolytic stability of purified proteins was frequently affected by the methodology used for protein purification and the ratio of protens to digestive enzymes used in the assays. Nowadays, the scientific community thrives to establish in vitro digestion protocols that mimic physiological conditions and take into account complex compositon of the food. New studies support this tendency, since it was shown that the presence of various biomolecules in food matrix affects the proteolysis in the simulated gastrointestinal conditions. On top of that, survival of intact proteins upon proteolysis seems not to be necessary, but frequently protein fragments of higher molecular weight with partially preserved structure might be enough to elicit allergic reaction in sensitized individuals.
PB  - New York : Nova Science Publishers
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Food Allergens’ Susceptibility to Proteolysis
SP  - 220
VL  - 6
UR  - https://hdl.handle.net/21.15107/rcub_intor_765
ER  - 
@inbook{
author = "Prodić, Ivana and Smiljanić, Katarina and Radosavljević, Jelena",
year = "2020",
abstract = "Common properties of food allergens are prominent resistance to heat treatment and enzyme proteolysis. Stability of the proteins upon gastrointestinal proteolysis of food highly correlates with its allergenic potential. At this moment, the scientific community is putting a lot of effort to connect the available knowledge on the structure and function of food proteins, with stability to proteolysis in order to provide the most reliable prediction tool for allergenicity of novel proteins. Moreover, choosing the conditions under which gastrointestinal proteolysis is simulated may profoundly affect the results of assays and allergenicity assessment. At the beginning of research, for the link between allergenicity and proteolytic stability, purified allergens were used. However, this approchad was proved to be prone to production of erroneous data, since the proteolytic stability of purified proteins was frequently affected by the methodology used for protein purification and the ratio of protens to digestive enzymes used in the assays. Nowadays, the scientific community thrives to establish in vitro digestion protocols that mimic physiological conditions and take into account complex compositon of the food. New studies support this tendency, since it was shown that the presence of various biomolecules in food matrix affects the proteolysis in the simulated gastrointestinal conditions. On top of that, survival of intact proteins upon proteolysis seems not to be necessary, but frequently protein fragments of higher molecular weight with partially preserved structure might be enough to elicit allergic reaction in sensitized individuals.",
publisher = "New York : Nova Science Publishers",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Food Allergens’ Susceptibility to Proteolysis",
pages = "220",
volume = "6",
url = "https://hdl.handle.net/21.15107/rcub_intor_765"
}
Prodić, I., Smiljanić, K.,& Radosavljević, J.. (2020). Food Allergens’ Susceptibility to Proteolysis. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publishers., 6, 220.
https://hdl.handle.net/21.15107/rcub_intor_765
Prodić I, Smiljanić K, Radosavljević J. Food Allergens’ Susceptibility to Proteolysis. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;6:220.
https://hdl.handle.net/21.15107/rcub_intor_765 .
Prodić, Ivana, Smiljanić, Katarina, Radosavljević, Jelena, "Food Allergens’ Susceptibility to Proteolysis" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 6 (2020):220,
https://hdl.handle.net/21.15107/rcub_intor_765 .

Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu

Prodić, Ivana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Prodić, Ivana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7705
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22917/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23935753
UR  - https://nardus.mpn.gov.rs/handle/123456789/17617
UR  - http://intor.torlakinstitut.com/handle/123456789/777
AB  - INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije.
AB  - INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu
UR  - https://hdl.handle.net/21.15107/rcub_intor_777
ER  - 
@phdthesis{
author = "Prodić, Ivana",
year = "2019",
abstract = "INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije., INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu",
url = "https://hdl.handle.net/21.15107/rcub_intor_777"
}
Prodić, I.. (2019). Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_intor_777
Prodić I. Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_intor_777 .
Prodić, Ivana, "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_intor_777 .

Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products

Prodić, Ivana; Smiljanić, Katarina; Mihailović, Jelena; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(Univerzitet u Beogradu - Hemijski fakultet, 2019)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/775
AB  - Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products
EP  - 25
SP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_intor_775
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Mihailović, Jelena and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_intor_775"
}
Prodić, I., Smiljanić, K., Mihailović, J., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2019). Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet., 25-25.
https://hdl.handle.net/21.15107/rcub_intor_775
Prodić I, Smiljanić K, Mihailović J, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;:25-25.
https://hdl.handle.net/21.15107/rcub_intor_775 .
Prodić, Ivana, Smiljanić, Katarina, Mihailović, Jelena, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019 (2019):25-25,
https://hdl.handle.net/21.15107/rcub_intor_775 .

Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)

Mihailović, Jelena; Prodić, Ivana; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Serbian Proteomic Association - SePA, 2019)

TY  - CONF
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/770
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions rangingfrom mild to severe. Major peanut allergen IgE epitopes are well characterized but little is knownabout their post-translational modifications (PTM) and how they are affected by thermaltreatment. PTM profile may differ between raw and thermally treated peanut, which could affectits allergic potential depending on type, size and position of modifications.Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-upproteomics methods.Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digestedin gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (ThermoFisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 andAra h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the ImmuneEpitope Database (IEDB www.iedb.org).Main findings. LFQ results show that there is no significant change in the amountsof any of thestudied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in thehighest portion, with respect to the protein size: 15% and 12% of its positions are modified in rawand roasted sample, respectively. Total of 21 modifications were quantified between the twopreparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largestnumber of peptides.Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern andquantity between treated and non-treated extracts. The in silico discovered PTMs could affectprotein digestibility and allergenicity. Further investigation is necessary in order to fully understandthe impact protein modifications could have on their allergenic potential.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
T1  - Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
SP  - 16/L10
UR  - https://hdl.handle.net/21.15107/rcub_intor_770
ER  - 
@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions rangingfrom mild to severe. Major peanut allergen IgE epitopes are well characterized but little is knownabout their post-translational modifications (PTM) and how they are affected by thermaltreatment. PTM profile may differ between raw and thermally treated peanut, which could affectits allergic potential depending on type, size and position of modifications.Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-upproteomics methods.Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digestedin gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (ThermoFisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 andAra h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the ImmuneEpitope Database (IEDB www.iedb.org).Main findings. LFQ results show that there is no significant change in the amountsof any of thestudied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in thehighest portion, with respect to the protein size: 15% and 12% of its positions are modified in rawand roasted sample, respectively. Total of 21 modifications were quantified between the twopreparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largestnumber of peptides.Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern andquantity between treated and non-treated extracts. The in silico discovered PTMs could affectprotein digestibility and allergenicity. Further investigation is necessary in order to fully understandthe impact protein modifications could have on their allergenic potential.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019",
title = "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
pages = "16/L10",
url = "https://hdl.handle.net/21.15107/rcub_intor_770"
}
Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA., 16/L10.
https://hdl.handle.net/21.15107/rcub_intor_770
Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019. 2019;:16/L10.
https://hdl.handle.net/21.15107/rcub_intor_770 .
Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019 (2019):16/L10,
https://hdl.handle.net/21.15107/rcub_intor_770 .

In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljković, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Wiley, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljković, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/763
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress
EP  - 878
IS  - supp. 106
SP  - 878
VL  - 74
UR  - https://hdl.handle.net/21.15107/rcub_intor_763
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljković, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress",
pages = "878-878",
number = "supp. 106",
volume = "74",
url = "https://hdl.handle.net/21.15107/rcub_intor_763"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljković, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74(supp. 106), 878-878.
https://hdl.handle.net/21.15107/rcub_intor_763
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljković Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74(supp. 106):878-878.
https://hdl.handle.net/21.15107/rcub_intor_763 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljković, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress" in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74, no. supp. 106 (2019):878-878,
https://hdl.handle.net/21.15107/rcub_intor_763 .

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/536
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
EP  - 658
SP  - 644
VL  - 126
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
pages = "658-644",
volume = "126",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Pergamon-Elsevier Science Ltd, Oxford., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer L, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija, Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .
2
15
5
15

Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Radosavljević, Jelena; Mihailović, Jelena; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Srpsko Udruženje za Proteomiku; IBISS, 2018)

TY  - CONF
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Radosavljević, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/789
AB  - Objective: Major peanut allergens, Ara h 2 and Ara h 6, are known to be resistant to pepsindigestion, and they sensitize individual via the gastrointestinal tract. Mikenus et al. published astandardized static digestion method for food, based on physiological conditions emphasizing theimpact of food matrices. Immunoreactive proteins (large fragments) and peptides (short digestionresistant peptides SDRPs; <10 kDa), to which the immune system of the gastrointestinal tract isexposed during digestion of peanut proteins, has not been investigated under pure physiologicalconditions suggested by this protocol.Matherial and methods: Whole grain of grounded raw peanut was incubated with human α-amylase, and pepsin, mimicking the effects of oral and gastric digestion, in total duration of 2h.Bottom up proteomic approach, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, wereused to identify and characterize peanut digesta.Results: After 2h of oral/gastric phase we got, intact proteins, large, digestion resistant peptides(DRP) and SDRPs, as well. Ara h 2 and Ara h 6 remained mostly intact, and short DRPs from Ara h2 and Ara h 6 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h3 showed preserved allergenic capacity, as well. Almost all of identified short DRPs from Ara h 1,Ara h 2 and Ara h 3, with preserved allergenic potential, were constituents of continuous epitopesequences found via Immune Epitope Database (www.iedb.org).Conclusion: Processes of protein extraction from the matrix and their enzymatic digestion occursimultaneously. Oral and gastric phase digestion products of raw peanut are intact proteins, largeand short digestion resistant peptides. Under these conditions Ara h 2 and Ara h 6 are expectedly
PB  - Srpsko Udruženje za Proteomiku; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix
UR  - https://hdl.handle.net/21.15107/rcub_intor_789
ER  - 
@conference{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Radosavljević, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Major peanut allergens, Ara h 2 and Ara h 6, are known to be resistant to pepsindigestion, and they sensitize individual via the gastrointestinal tract. Mikenus et al. published astandardized static digestion method for food, based on physiological conditions emphasizing theimpact of food matrices. Immunoreactive proteins (large fragments) and peptides (short digestionresistant peptides SDRPs; <10 kDa), to which the immune system of the gastrointestinal tract isexposed during digestion of peanut proteins, has not been investigated under pure physiologicalconditions suggested by this protocol.Matherial and methods: Whole grain of grounded raw peanut was incubated with human α-amylase, and pepsin, mimicking the effects of oral and gastric digestion, in total duration of 2h.Bottom up proteomic approach, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, wereused to identify and characterize peanut digesta.Results: After 2h of oral/gastric phase we got, intact proteins, large, digestion resistant peptides(DRP) and SDRPs, as well. Ara h 2 and Ara h 6 remained mostly intact, and short DRPs from Ara h2 and Ara h 6 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h3 showed preserved allergenic capacity, as well. Almost all of identified short DRPs from Ara h 1,Ara h 2 and Ara h 3, with preserved allergenic potential, were constituents of continuous epitopesequences found via Immune Epitope Database (www.iedb.org).Conclusion: Processes of protein extraction from the matrix and their enzymatic digestion occursimultaneously. Oral and gastric phase digestion products of raw peanut are intact proteins, largeand short digestion resistant peptides. Under these conditions Ara h 2 and Ara h 6 are expectedly",
publisher = "Srpsko Udruženje za Proteomiku; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix",
url = "https://hdl.handle.net/21.15107/rcub_intor_789"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Radosavljević, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku; IBISS..
https://hdl.handle.net/21.15107/rcub_intor_789
Prodić I, Stanić-Vučinić D, Apostolović D, Radosavljević J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;.
https://hdl.handle.net/21.15107/rcub_intor_789 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Radosavljević, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018),
https://hdl.handle.net/21.15107/rcub_intor_789 .

Digestomics of Japanese abalone in real food matrix

Prodić, Ivana; Khulal, Urmila; Mutić, Jelena; Mihailović, Jelena; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Srpsko Udruženje za Proteomiku, SePA; IBISS, 2018)

TY  - CONF
AU  - Prodić, Ivana
AU  - Khulal, Urmila
AU  - Mutić, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/774
AB  - Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highlynutritive food resource in the world, but also among the eight allergic food groups accounting forapproximately 90% of all immunoglobulin E food allergies worldwide. The general objective of ourresearch is to comprehensively investigate stability and structures of pepsin-resistant allergens, oftheir larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsindigestion of whole raw and extract of shellfish, under standardized and physiologically relevantgastric conditions.Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),were pepsin digested according to standardized static digestion protocol. Controls were treated in asame manner without adding pepsin. Supernatant of samples and its counterpart controls wereprecipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed byncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQalgorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,Canada.Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed arange of proteins in varied concentrations between 10-250 kDa. In extracted and whole rawshellfish, approximately 22 prominent protein bands were observed including the distinct bandscorresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,specifically around the low molecular weight protein bands. The smearing could possibly be due tothe breakdown products and the glycation. There were slight differences between the proteinprofiles under reducing and non-reducing conditions as well. Nevertheless, there was the retentionof a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stabletropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di1), with 90% of sequence homology with main tropomyosin allergens from seafood.Scientific impact and relevance: The results will highlight effects of food matrix on shellfishallergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will beobtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in thereal food matrix.
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Digestomics of Japanese abalone in real food matrix
EP  - 10
SP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_intor_774
ER  - 
@conference{
author = "Prodić, Ivana and Khulal, Urmila and Mutić, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highlynutritive food resource in the world, but also among the eight allergic food groups accounting forapproximately 90% of all immunoglobulin E food allergies worldwide. The general objective of ourresearch is to comprehensively investigate stability and structures of pepsin-resistant allergens, oftheir larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsindigestion of whole raw and extract of shellfish, under standardized and physiologically relevantgastric conditions.Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),were pepsin digested according to standardized static digestion protocol. Controls were treated in asame manner without adding pepsin. Supernatant of samples and its counterpart controls wereprecipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed byncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQalgorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,Canada.Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed arange of proteins in varied concentrations between 10-250 kDa. In extracted and whole rawshellfish, approximately 22 prominent protein bands were observed including the distinct bandscorresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,specifically around the low molecular weight protein bands. The smearing could possibly be due tothe breakdown products and the glycation. There were slight differences between the proteinprofiles under reducing and non-reducing conditions as well. Nevertheless, there was the retentionof a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stabletropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di1), with 90% of sequence homology with main tropomyosin allergens from seafood.Scientific impact and relevance: The results will highlight effects of food matrix on shellfishallergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will beobtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in thereal food matrix.",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Digestomics of Japanese abalone in real food matrix",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_intor_774"
}
Prodić, I., Khulal, U., Mutić, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 10-10.
https://hdl.handle.net/21.15107/rcub_intor_774
Prodić I, Khulal U, Mutić J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:10-10.
https://hdl.handle.net/21.15107/rcub_intor_774 .
Prodić, Ivana, Khulal, Urmila, Mutić, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Digestomics of Japanese abalone in real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):10-10,
https://hdl.handle.net/21.15107/rcub_intor_774 .

Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion

Prodić, Ivana; Dubiela, Pawel; Mihailović, Jelena; Stanić-Vučinić, Dragana; Smiljanić, Katarina; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(IMPARAS Cost Action FA1402, 2018)

TY  - CONF
AU  - Prodić, Ivana
AU  - Dubiela, Pawel
AU  - Mihailović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/776
AB  - Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.
PB  - IMPARAS Cost Action FA1402
C3  - Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018
T1  - Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion
EP  - 59
SP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_intor_776
ER  - 
@conference{
author = "Prodić, Ivana and Dubiela, Pawel and Mihailović, Jelena and Stanić-Vučinić, Dragana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.",
publisher = "IMPARAS Cost Action FA1402",
journal = "Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018",
title = "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_intor_776"
}
Prodić, I., Dubiela, P., Mihailović, J., Stanić-Vučinić, D., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2018). Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018
IMPARAS Cost Action FA1402., 59-59.
https://hdl.handle.net/21.15107/rcub_intor_776
Prodić I, Dubiela P, Mihailović J, Stanić-Vučinić D, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018. 2018;:59-59.
https://hdl.handle.net/21.15107/rcub_intor_776 .
Prodić, Ivana, Dubiela, Pawel, Mihailović, Jelena, Stanić-Vučinić, Dragana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion" in Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018 (2018):59-59,
https://hdl.handle.net/21.15107/rcub_intor_776 .

Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination

Smiljanić, Katarina; Prodić, Ivana; Aleksić, Ivana; Veljović, Đorđe; Ćirković-Veličković, Tanja; Mutić, Jelena; Burazer, Lidija M.

(Srpsko Udruženje za Proteomiku, SePA; IBISS, 2018)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Aleksić, Ivana
AU  - Veljović, Đorđe
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Burazer, Lidija M.
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/772
AB  - Objective: to create method for unrestrictive deep, relative quantification of post translationalmodifications (PTMs) within different proteomes. Pollution field studies of bio indicators such aspollen are valuable because of realistic situation of target contamination, however they carry thegreat extent of uncertainty in attributing and delineating the polluting effect from multiple sources.Holistic research platform focusing on comprehensively characterized and quantified PTMs ofcomparable bio-indicator proteomes could help and overcome these obstacles of field pollutionstudies.Material and Methods: Scanning electron and light microscopy assessed surface and sub pollenparticle (SPP) releasing features of timothy grass (TG) pollen. Inductively coupled atomic emissionspectrometry revealed metal elemental content in pollen while in solution trypsin digested pollenproteomes analysed with high resolution Orbitrap mass tandem spectrometry and PEAKS Suite 8.5brought quantitative information on protein expression level and its PTM profiling.Results: TG polluted pollen samples (P2) collected along regional road and chemical plant,exposed to air contaminants from road traffics and chemical plants showed 4.5 times higher SPPreleasing capacity, with notable surface changes, as well as significantly higher contents of Mn, Hgand Cd. Antioxidative enzymes (oxidoreductases, superoxide dismutases and peroxidases),including actin, were upregulated several times in polluted sample compared to ecologicallypreserved pollen (P1). While the level of spontaneous and physiological PTMs includingmethylation, acetylation, deamidation and formylation, was similar without significant changes inP1 and P2 pollens, oxidative PTMs including oxidation of Met, Lys, His, Pro and HNE and hexoseadducts showed several times higher and significant increase in abundancy of P2 compared to P1.PTMs connected to road traffic such as tyrosine nitration were very rare and low abundant.Conclusion: Results suggest prominent role of chemical pollution compared to effect of road trafficpollution, with primary consequences from oxidative properties of mercury (Hg) and cadmium(Cd).
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination
EP  - 13
SP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_intor_772
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Aleksić, Ivana and Veljović, Đorđe and Ćirković-Veličković, Tanja and Mutić, Jelena and Burazer, Lidija M.",
year = "2018",
abstract = "Objective: to create method for unrestrictive deep, relative quantification of post translationalmodifications (PTMs) within different proteomes. Pollution field studies of bio indicators such aspollen are valuable because of realistic situation of target contamination, however they carry thegreat extent of uncertainty in attributing and delineating the polluting effect from multiple sources.Holistic research platform focusing on comprehensively characterized and quantified PTMs ofcomparable bio-indicator proteomes could help and overcome these obstacles of field pollutionstudies.Material and Methods: Scanning electron and light microscopy assessed surface and sub pollenparticle (SPP) releasing features of timothy grass (TG) pollen. Inductively coupled atomic emissionspectrometry revealed metal elemental content in pollen while in solution trypsin digested pollenproteomes analysed with high resolution Orbitrap mass tandem spectrometry and PEAKS Suite 8.5brought quantitative information on protein expression level and its PTM profiling.Results: TG polluted pollen samples (P2) collected along regional road and chemical plant,exposed to air contaminants from road traffics and chemical plants showed 4.5 times higher SPPreleasing capacity, with notable surface changes, as well as significantly higher contents of Mn, Hgand Cd. Antioxidative enzymes (oxidoreductases, superoxide dismutases and peroxidases),including actin, were upregulated several times in polluted sample compared to ecologicallypreserved pollen (P1). While the level of spontaneous and physiological PTMs includingmethylation, acetylation, deamidation and formylation, was similar without significant changes inP1 and P2 pollens, oxidative PTMs including oxidation of Met, Lys, His, Pro and HNE and hexoseadducts showed several times higher and significant increase in abundancy of P2 compared to P1.PTMs connected to road traffic such as tyrosine nitration were very rare and low abundant.Conclusion: Results suggest prominent role of chemical pollution compared to effect of road trafficpollution, with primary consequences from oxidative properties of mercury (Hg) and cadmium(Cd).",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_intor_772"
}
Smiljanić, K., Prodić, I., Aleksić, I., Veljović, Đ., Ćirković-Veličković, T., Mutić, J.,& Burazer, L. M.. (2018). Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 13-13.
https://hdl.handle.net/21.15107/rcub_intor_772
Smiljanić K, Prodić I, Aleksić I, Veljović Đ, Ćirković-Veličković T, Mutić J, Burazer LM. Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:13-13.
https://hdl.handle.net/21.15107/rcub_intor_772 .
Smiljanić, Katarina, Prodić, Ivana, Aleksić, Ivana, Veljović, Đorđe, Ćirković-Veličković, Tanja, Mutić, Jelena, Burazer, Lidija M., "Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):13-13,
https://hdl.handle.net/21.15107/rcub_intor_772 .

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, M.; Radosavljević, Jelena; Burazer, Lidija; Milcić, M.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Radibratović, M.
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Milcić, M.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/608
AB  - Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
EP  - 740
IS  - 6
SP  - 731
VL  - 48
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović, Jelena and Radibratović, M. and Radosavljević, Jelena and Burazer, Lidija and Milcić, M. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
pages = "740-731",
number = "6",
volume = "48",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović, J., Radibratović, M., Radosavljević, J., Burazer, L., Milcić, M., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović J, Radibratović M, Radosavljević J, Burazer L, Milcić M, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović, Jelena, Radibratović, M., Radosavljević, Jelena, Burazer, Lidija, Milcić, M., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .
3
40
24
41

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, M.; Radosavljević, Jelena; Burazer, Lidija; Milcić, M.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Radibratović, M.
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Milcić, M.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/514
AB  - Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
EP  - 740
IS  - 6
SP  - 731
VL  - 48
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović, Jelena and Radibratović, M. and Radosavljević, Jelena and Burazer, Lidija and Milcić, M. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
pages = "740-731",
number = "6",
volume = "48",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović, J., Radibratović, M., Radosavljević, J., Burazer, L., Milcić, M., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović J, Radibratović M, Radosavljević J, Burazer L, Milcić M, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović, Jelena, Radibratović, M., Radosavljević, Jelena, Burazer, Lidija, Milcić, M., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .
3
40
24
41

Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Perusko, Marija; Al-Hanish, Ayah; Mihailović, Jelena; Minić, Simeon; Trifunović, Sara; Prodić, Ivana; Cirkovic Velicković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - JOUR
AU  - Perusko, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović, Jelena
AU  - Minić, Simeon
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Cirkovic Velicković, Tanja
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/757
AB  - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
EP  - 752
SP  - 744
VL  - 232
DO  - 10.1016/j.foodchem.2017.04.074
ER  - 
@article{
author = "Perusko, Marija and Al-Hanish, Ayah and Mihailović, Jelena and Minić, Simeon and Trifunović, Sara and Prodić, Ivana and Cirkovic Velicković, Tanja",
year = "2017",
abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction",
pages = "752-744",
volume = "232",
doi = "10.1016/j.foodchem.2017.04.074"
}
Perusko, M., Al-Hanish, A., Mihailović, J., Minić, S., Trifunović, S., Prodić, I.,& Cirkovic Velicković, T.. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 232, 744-752.
https://doi.org/10.1016/j.foodchem.2017.04.074
Perusko M, Al-Hanish A, Mihailović J, Minić S, Trifunović S, Prodić I, Cirkovic Velicković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry. 2017;232:744-752.
doi:10.1016/j.foodchem.2017.04.074 .
Perusko, Marija, Al-Hanish, Ayah, Mihailović, Jelena, Minić, Simeon, Trifunović, Sara, Prodić, Ivana, Cirkovic Velicković, Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" in Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 . .
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Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/759
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
EP  - 250
SP  - 241
VL  - 61
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 
@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
pages = "250-241",
volume = "61",
doi = "10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T.. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids. 2016;61:241-250.
doi:10.1016/j.foodhyd.2016.05.012 .
Al-Hanish, Ayah, Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Prodić, Ivana, Minić, Simeon L., Stojadinović, Marija M., Radibratović, Milica, Milčić, Miloš K., Ćirković-Veličković, Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" in Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 . .
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