Enzyme inhibition, molecular docking, and density functional theory studies of new thiosemicarbazones incorporating the 4‐hydroxy‐3,5‐dimethoxy benzaldehyde motif
Yazarlar (7)
Profesör Yeliz Demir
Ardahan Üniversitesi, Türkiye
Cüneyt Türkeş
Erzincan Binali Yıldırım Üniversitesi, Türkiye
Muhammet S. Çavuş
Kastamonu University, Türkiye
Doç. Dr. Musa ERDOĞAN
Kafkas Üniversitesi, Türkiye
Halit Muğlu
Kastamonu University, Türkiye
Hasan Yakan
Ondokuz Mayis Üniversitesi, Türkiye
Şükrü Beydemir
Anadolu Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Archiv Der Pharmazie (Q1) | ||
| Dergi ISSN | 0365-6233 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 04-2023 |
| Cilt / Sayı / Sayfa | 356 / 4 / – | DOI | 10.1002/ardp.202200554 |
| Makale Linki | http://dx.doi.org/10.1002/ardp.202200554 | ||
| Özet |
| New Schiff base-bearing thiosemicarbazones (1–13) were obtained from 4-hydroxy-3,5-dimethoxy benzaldehyde and various isocyanates. The structures of the synthesized molecules were elucidated in detail. Density functional theory calculations were also performed to determine the spectroscopic properties of the compounds. Moreover, the enzyme inhibition activities of these compounds were investigated. They showed highly potent inhibition effects on acetylcholinesterase (AChE) and human carbonic anhydrases (hCAs) (KI values are in the range of 51.11 ± 6.01 to 278.10 ± 40.55 nM, 60.32 ± 9.78 to 300.00 ± 77.41 nM, and 64.21 ± 9.99 to 307.70 ± 61.35 nM for AChE, hCA I, and hCA II, respectively). In addition, molecular docking studies were performed, confirmed by binding affinities studies of the most potent derivatives. |
| Anahtar Kelimeler |
| DFT | enzyme inhibition | molecular docking | spectroscopic elucidation | thiosemicarbazones |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| SCOPUS | 63 |
| Google Scholar | 63 |