| Yazarlar (7) |
Betül Kaya
Türkiye |
|
Hakan Tahtacı
Türkiye |
|
Bilge Çiftci
Türkiye |
Doç. Dr. Hatice Esra DURAN
Kafkas Üniversitesi, Türkiye |
|
Adem Necip
Türkiye |
|
Mesut Işık
Bilecik Şeyh Edebali Üniversitesi, Türkiye |
|
Şükrü Beydemir
Anadolu Üniversitesi, Türkiye |
| Özet |
| In this study, hydrazine clubbed thiazole derivatives (3a-3j) were obtained by Hantzsch thiazole synthesis and characterized by MS, H NMR, and C NMR. The inhibitory potentials of the derivatives against diabetes-related enzymes such as aldose reductase (AR), α-glycosidase (α-GLY), and α-amylase (α-AMY) were experimentally determined, and the results were supported by molecular docking. The results showed that the derivatives (3a-3j) displayed varied degree of potential inhibitory activity, with K values covering the following ranges: 5.47 ± 0.53 to 23.89 ± 1.46 nM for AR and 1.76 ± 0.01 to 24.81 ± 0.15 μM for α-GLY, and with IC values 4.94-28.17 μM for α-AMY, as compared to standard epalrestat and acarbose (K: 34.53 ± 2.52 nM for AR and 23.53 ± 2.72 μM for α-GLY, respectively). The selective activity of these derivatives on antidiabetic enzymes may be important for the treatment of diabetes and may lead to the development of alternative new compounds for this purpose. |
| Anahtar Kelimeler |
| ADME | aldose reductase | alpha-amylase | alpha-glucosidase | antidiabetic | molecular docking | thiazole |
| Makale Türü |
Özgün Makale
|
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale |
| Dergi Adı | Drug Development Research |
| Dergi ISSN | 0272-4391 Wos Dergi Scopus Dergi |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q1 |
| Makale Dili | Türkçe |
| Basım Tarihi | 02-2025 |
| Cilt No | 86 |
| Sayı | 1 |
| Doi Numarası | 10.1002/ddr.70060 |
| Makale Linki | https://doi.org/10.1002/ddr.70060 |
| Atıf Sayıları | |
| WoS | 5 |
| Google Scholar | 7 |
