| Yazarlar |
Zuhal ALIM
Kırşehir Ahi Evran Üniversitesi, Türkiye |
Turgay TUNÇ
Kırşehir Ahi Evran Üniversitesi, Türkiye |
Nadir DEMİREL
Kırşehir Ahi Evran Üniversitesi, Türkiye |
Aslıhan GÜNEL
Kırşehir Ahi Evran Üniversitesi, Türkiye |
Nurcan Karacan
Gazi Üniversitesi, Türkiye |
| Özet |
| Acetylcholinesterase (AChE) and carbonic anhydrase I (CA-I) and II (CA-II) are two vital metabolic enzymes. AChE inhibitors are seen as target molecules in drug development studies for Alzheimer's treatment. CA inhibitors are target molecules for treating many diseases from glaucoma to cancer. For this reason, it is crucial to identify new AChE and CA inhibitors. In this study, four benzimidazole acetamide derivatives were synthesized and their inhibition effects were investigated against human erythrocyte carbonic anhydrase I (hCA-I), II (hCA-II), and AChE. IC50 values of 9a-10b were determined in the range of 0.936 to 17.07 mu M for AChE. IC50 values of 9a-10b for hCA-I were found as 7.21 mu M, 4.72 mu M, 6.08 mu M, 8.23 mu M, respectively. On the other hand, IC50 values of 9a-9b for hCA-II were found as 8.64 mu M, 7.07 mu M, 4.12 mu M, 5.93 mu M, respectively. According to IC50 values, 9a -10b molecules exhibited strong inhibition effects for AChE and hCAI, II. Also, Molecular docking studies were carried out to explain the binding interaction of 9a -10b with AChE, hCA-I, and hCA-II. (C) 2022 Elsevier B.V. All rights reserved. |
| Anahtar Kelimeler |
| Acetylcholinesterase | Benzimidazole | Carbonic anhydrase | Inhibition | Molecular docking |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale |
| Dergi Adı | JOURNAL OF MOLECULAR STRUCTURE |
| Dergi ISSN | 0022-2860 |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q2 |
| Makale Dili | Türkçe |
| Basım Tarihi | 11-2022 |
| Cilt No | 1268 |
| Sayı | 1 |
| Doi Numarası | 10.1016/j.molstruc.2022.133647 |
| Makale Linki | http://dx.doi.org/10.1016/j.molstruc.2022.133647 |
| Atıf Sayıları | |
| WoS | 8 |
| SCOPUS | 7 |
| Google Scholar | 10 |
