Tomović, Katarina

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  • Tomović, Katarina (3)
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Author's Bibliography

Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors

Tomović, Katarina; Ilić, Budimir S.; Smelcerović, Zaklina; Miljković, Marija; Yancheva, Denitsa; Kojić, Milan; Mavrova, Anelia Ts; Kocić, Gordana; Smelcerović, Andrija

(Elsevier Ireland Ltd, Clare, 2020)

TY  - JOUR
AU  - Tomović, Katarina
AU  - Ilić, Budimir S.
AU  - Smelcerović, Zaklina
AU  - Miljković, Marija
AU  - Yancheva, Denitsa
AU  - Kojić, Milan
AU  - Mavrova, Anelia Ts
AU  - Kocić, Gordana
AU  - Smelcerović, Andrija
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1376
UR  - http://intor.torlakinstitut.com/handle/123456789/699
AB  - Multiple-targeting compounds might reduce complex polypharmacy of multifactorial diseases, such as diabetes, and contribute to the greater therapeutic success. Targeting reactive oxygen species-producing enzymes, as xanthine oxidase (XO), might suppress progression of diabetes-associated vascular complications. In this study a small series of benzimidazole derivatives (1-9) was evaluated for inhibitory activity against dipeptidyl peptidase-4 (DPP-4) and XO. One 1,3-disubstituted-benzimidazole-2-imine (5) and 1,3-thiazolo [3,2-a] benzimidazolone derivative (8) were shown as effective dual DPP-4 and XO inhibitors, with IC50 values lower than 200 mu M, and predicted binding modes with both target enzymes. Both selected dual inhibitors (compounds 5 and 8) did not show cytotoxicity to a greater extent on Caco-2 cells even at concentration of 250 mu M. These structures represent new non-purine scaffolds bearing two therapeutic functionalities, being DPP-4 and XO inhibitors, more favorable in comparison to DPP-4 inhibitors with DPP-4 as a single target due to pleiotropic effects of XO inhibition.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors
VL  - 315
DO  - 10.1016/j.cbi.2019.108873
ER  - 
@article{
author = "Tomović, Katarina and Ilić, Budimir S. and Smelcerović, Zaklina and Miljković, Marija and Yancheva, Denitsa and Kojić, Milan and Mavrova, Anelia Ts and Kocić, Gordana and Smelcerović, Andrija",
year = "2020",
abstract = "Multiple-targeting compounds might reduce complex polypharmacy of multifactorial diseases, such as diabetes, and contribute to the greater therapeutic success. Targeting reactive oxygen species-producing enzymes, as xanthine oxidase (XO), might suppress progression of diabetes-associated vascular complications. In this study a small series of benzimidazole derivatives (1-9) was evaluated for inhibitory activity against dipeptidyl peptidase-4 (DPP-4) and XO. One 1,3-disubstituted-benzimidazole-2-imine (5) and 1,3-thiazolo [3,2-a] benzimidazolone derivative (8) were shown as effective dual DPP-4 and XO inhibitors, with IC50 values lower than 200 mu M, and predicted binding modes with both target enzymes. Both selected dual inhibitors (compounds 5 and 8) did not show cytotoxicity to a greater extent on Caco-2 cells even at concentration of 250 mu M. These structures represent new non-purine scaffolds bearing two therapeutic functionalities, being DPP-4 and XO inhibitors, more favorable in comparison to DPP-4 inhibitors with DPP-4 as a single target due to pleiotropic effects of XO inhibition.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors",
volume = "315",
doi = "10.1016/j.cbi.2019.108873"
}
Tomović, K., Ilić, B. S., Smelcerović, Z., Miljković, M., Yancheva, D., Kojić, M., Mavrova, A. T., Kocić, G.,& Smelcerović, A.. (2020). Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 315.
https://doi.org/10.1016/j.cbi.2019.108873
Tomović K, Ilić BS, Smelcerović Z, Miljković M, Yancheva D, Kojić M, Mavrova AT, Kocić G, Smelcerović A. Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors. in Chemico-Biological Interactions. 2020;315.
doi:10.1016/j.cbi.2019.108873 .
Tomović, Katarina, Ilić, Budimir S., Smelcerović, Zaklina, Miljković, Marija, Yancheva, Denitsa, Kojić, Milan, Mavrova, Anelia Ts, Kocić, Gordana, Smelcerović, Andrija, "Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors" in Chemico-Biological Interactions, 315 (2020),
https://doi.org/10.1016/j.cbi.2019.108873 . .
10
13

Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors

Tomović, Katarina; Ilić, Budimir S.; Smelcerović, Zaklina; Miljković, Marija; Yancheva, Denitsa; Kojić, Milan; Mavrova, Anelia Ts; Kocić, Gordana; Smelcerović, Andrija

(Elsevier Ireland Ltd, Clare, 2020)

TY  - JOUR
AU  - Tomović, Katarina
AU  - Ilić, Budimir S.
AU  - Smelcerović, Zaklina
AU  - Miljković, Marija
AU  - Yancheva, Denitsa
AU  - Kojić, Milan
AU  - Mavrova, Anelia Ts
AU  - Kocić, Gordana
AU  - Smelcerović, Andrija
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1376
UR  - http://intor.torlakinstitut.com/handle/123456789/698
AB  - Multiple-targeting compounds might reduce complex polypharmacy of multifactorial diseases, such as diabetes, and contribute to the greater therapeutic success. Targeting reactive oxygen species-producing enzymes, as xanthine oxidase (XO), might suppress progression of diabetes-associated vascular complications. In this study a small series of benzimidazole derivatives (1-9) was evaluated for inhibitory activity against dipeptidyl peptidase-4 (DPP-4) and XO. One 1,3-disubstituted-benzimidazole-2-imine (5) and 1,3-thiazolo [3,2-a] benzimidazolone derivative (8) were shown as effective dual DPP-4 and XO inhibitors, with IC50 values lower than 200 mu M, and predicted binding modes with both target enzymes. Both selected dual inhibitors (compounds 5 and 8) did not show cytotoxicity to a greater extent on Caco-2 cells even at concentration of 250 mu M. These structures represent new non-purine scaffolds bearing two therapeutic functionalities, being DPP-4 and XO inhibitors, more favorable in comparison to DPP-4 inhibitors with DPP-4 as a single target due to pleiotropic effects of XO inhibition.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors
VL  - 315
DO  - 10.1016/j.cbi.2019.108873
ER  - 
@article{
author = "Tomović, Katarina and Ilić, Budimir S. and Smelcerović, Zaklina and Miljković, Marija and Yancheva, Denitsa and Kojić, Milan and Mavrova, Anelia Ts and Kocić, Gordana and Smelcerović, Andrija",
year = "2020",
abstract = "Multiple-targeting compounds might reduce complex polypharmacy of multifactorial diseases, such as diabetes, and contribute to the greater therapeutic success. Targeting reactive oxygen species-producing enzymes, as xanthine oxidase (XO), might suppress progression of diabetes-associated vascular complications. In this study a small series of benzimidazole derivatives (1-9) was evaluated for inhibitory activity against dipeptidyl peptidase-4 (DPP-4) and XO. One 1,3-disubstituted-benzimidazole-2-imine (5) and 1,3-thiazolo [3,2-a] benzimidazolone derivative (8) were shown as effective dual DPP-4 and XO inhibitors, with IC50 values lower than 200 mu M, and predicted binding modes with both target enzymes. Both selected dual inhibitors (compounds 5 and 8) did not show cytotoxicity to a greater extent on Caco-2 cells even at concentration of 250 mu M. These structures represent new non-purine scaffolds bearing two therapeutic functionalities, being DPP-4 and XO inhibitors, more favorable in comparison to DPP-4 inhibitors with DPP-4 as a single target due to pleiotropic effects of XO inhibition.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors",
volume = "315",
doi = "10.1016/j.cbi.2019.108873"
}
Tomović, K., Ilić, B. S., Smelcerović, Z., Miljković, M., Yancheva, D., Kojić, M., Mavrova, A. T., Kocić, G.,& Smelcerović, A.. (2020). Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 315.
https://doi.org/10.1016/j.cbi.2019.108873
Tomović K, Ilić BS, Smelcerović Z, Miljković M, Yancheva D, Kojić M, Mavrova AT, Kocić G, Smelcerović A. Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors. in Chemico-Biological Interactions. 2020;315.
doi:10.1016/j.cbi.2019.108873 .
Tomović, Katarina, Ilić, Budimir S., Smelcerović, Zaklina, Miljković, Marija, Yancheva, Denitsa, Kojić, Milan, Mavrova, Anelia Ts, Kocić, Gordana, Smelcerović, Andrija, "Benzimidazole-based dual dipeptidyl peptidase-4 and xanthine oxidase inhibitors" in Chemico-Biological Interactions, 315 (2020),
https://doi.org/10.1016/j.cbi.2019.108873 . .
10
13

Benzo[4,5]thieno[2,3-d]pyrimidine phthalimide derivative, one of the rare noncompetitive inhibitors of dipeptidyl peptidase-4

Tomović, Katarina; Ilić, Budimir S.; Miljković, Marija; Dimov, Stefan; Yancheva, Denitsa; Kojić, Milan; Mavrova, Anelia T.; Kocić, Gordana; Smelcerović, Andrija

(Wiley-V C H Verlag Gmbh, Weinheim, 2019)

TY  - JOUR
AU  - Tomović, Katarina
AU  - Ilić, Budimir S.
AU  - Miljković, Marija
AU  - Dimov, Stefan
AU  - Yancheva, Denitsa
AU  - Kojić, Milan
AU  - Mavrova, Anelia T.
AU  - Kocić, Gordana
AU  - Smelcerović, Andrija
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1396
UR  - http://intor.torlakinstitut.com/handle/123456789/700
AB  - A small library of benzo[4,5]thieno[2,3-d]pyrimidine phthalimide and amine derivatives was evaluated for inhibitory activity against dipeptidyl peptidase-4 (DPP-4). The phthalimide derivatives exhibited better activity than the amine precursors, with 2-(2-(3-chlorobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione (compound 14) as the most effective inhibitor (IC50 = 34.17 +/- 5.11 mu M). The five most potent selected inhibitors did not show cytotoxicity to a greater extent on Caco-2 cells, even at a concentration of 250 mu M. Compound 14 is considered as a novel representative of the rare noncompetitive DPP-4 inhibitors. Molecular docking and dynamics simulation indicated the importance of the Tyr547, Lys554, and Trp629 residues of DPP-4 in the formation of the enzyme-inhibitor complex. These observations could be potentially utilized for the rational design and optimization of novel (structurally similar, with phthalimide moiety, or different) noncompetitive DPP-4 inhibitors, which are anyway rare, but favorable in terms of the saturation of substrate competition.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Archiv Der Pharmazie
T1  - Benzo[4,5]thieno[2,3-d]pyrimidine phthalimide derivative, one of the rare noncompetitive inhibitors of dipeptidyl peptidase-4
IS  - 1
VL  - 353
DO  - 10.1002/ardp.201900238
ER  - 
@article{
author = "Tomović, Katarina and Ilić, Budimir S. and Miljković, Marija and Dimov, Stefan and Yancheva, Denitsa and Kojić, Milan and Mavrova, Anelia T. and Kocić, Gordana and Smelcerović, Andrija",
year = "2019",
abstract = "A small library of benzo[4,5]thieno[2,3-d]pyrimidine phthalimide and amine derivatives was evaluated for inhibitory activity against dipeptidyl peptidase-4 (DPP-4). The phthalimide derivatives exhibited better activity than the amine precursors, with 2-(2-(3-chlorobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione (compound 14) as the most effective inhibitor (IC50 = 34.17 +/- 5.11 mu M). The five most potent selected inhibitors did not show cytotoxicity to a greater extent on Caco-2 cells, even at a concentration of 250 mu M. Compound 14 is considered as a novel representative of the rare noncompetitive DPP-4 inhibitors. Molecular docking and dynamics simulation indicated the importance of the Tyr547, Lys554, and Trp629 residues of DPP-4 in the formation of the enzyme-inhibitor complex. These observations could be potentially utilized for the rational design and optimization of novel (structurally similar, with phthalimide moiety, or different) noncompetitive DPP-4 inhibitors, which are anyway rare, but favorable in terms of the saturation of substrate competition.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Archiv Der Pharmazie",
title = "Benzo[4,5]thieno[2,3-d]pyrimidine phthalimide derivative, one of the rare noncompetitive inhibitors of dipeptidyl peptidase-4",
number = "1",
volume = "353",
doi = "10.1002/ardp.201900238"
}
Tomović, K., Ilić, B. S., Miljković, M., Dimov, S., Yancheva, D., Kojić, M., Mavrova, A. T., Kocić, G.,& Smelcerović, A.. (2019). Benzo[4,5]thieno[2,3-d]pyrimidine phthalimide derivative, one of the rare noncompetitive inhibitors of dipeptidyl peptidase-4. in Archiv Der Pharmazie
Wiley-V C H Verlag Gmbh, Weinheim., 353(1).
https://doi.org/10.1002/ardp.201900238
Tomović K, Ilić BS, Miljković M, Dimov S, Yancheva D, Kojić M, Mavrova AT, Kocić G, Smelcerović A. Benzo[4,5]thieno[2,3-d]pyrimidine phthalimide derivative, one of the rare noncompetitive inhibitors of dipeptidyl peptidase-4. in Archiv Der Pharmazie. 2019;353(1).
doi:10.1002/ardp.201900238 .
Tomović, Katarina, Ilić, Budimir S., Miljković, Marija, Dimov, Stefan, Yancheva, Denitsa, Kojić, Milan, Mavrova, Anelia T., Kocić, Gordana, Smelcerović, Andrija, "Benzo[4,5]thieno[2,3-d]pyrimidine phthalimide derivative, one of the rare noncompetitive inhibitors of dipeptidyl peptidase-4" in Archiv Der Pharmazie, 353, no. 1 (2019),
https://doi.org/10.1002/ardp.201900238 . .
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