Discovery of Hydrazine Clubbed Thiazoles as Potential Antidiabetic Agents: Synthesis, Biological Evaluation, and Molecular Docking Studies
Yazarlar (7)
Doç. Dr. Betül Kaya Türkiye
Hakan Tahtacı Türkiye
Bilge Çiftci Türkiye
Doç. Dr. Hatice Esra DURAN Kafkas Üniversitesi, Türkiye
Dr. Öğr. Üyesi Adem Necip Türkiye
Prof. Dr. Mesut Işık Bilecik Şeyh Edebali Üniversitesi, Türkiye
Prof. Dr. Şükrü Beydemir Anadolu Üniversitesi, Türkiye
| Makale Türü |
Özgün Makale
(SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
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| Dergi Adı | DRUG DEVELOPMENT RESEARCH (Q1) | ||
| Dergi ISSN | 0272-4391 Dergi Bilgileri (2025) | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 02-2025 |
| Cilt / Sayı / Sayfa | 86 / 1 / – | DOI | 10.1002/ddr.70060 |
| Makale Linki | https://doi.org/10.1002/ddr.70060 | ||
| UAK Araştırma Alanları |
Tıbbi Biyokimya
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| Özet |
| In this study, hydrazine clubbed thiazole derivatives (3a–3j) were obtained by Hantzsch thiazole synthesis and characterized by MS, 1H NMR, and 13C 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 KI 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 IC50 values 4.94–28.17 μM for α‐AMY, as compared to standard epalrestat and acarbose (KI: 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 … |
| Anahtar Kelimeler |
| ADME | aldose reductase | alpha-amylase | alpha-glucosidase | antidiabetic | molecular docking | thiazole |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 10 |
| Google Scholar | 14 |