Molecular and structural characterization of ureido-benzenesulfonamides as dual inhibitors of aldose reductase and cholinesterases
Yazarlar (5)
Prof. Dr. Cüneyt Türkeş Erzincan Binali Yıldırım Üniversitesi, Türkiye
Doç. Dr. Nebih Lolak Adıyaman Üniversitesi, Türkiye
Doç. Dr. Hatice Esra DURAN Kafkas Üniversitesi, Türkiye
Doç. Dr. Gönül Yapar İstanbul Teknik Üniversitesi, Türkiye
Doç. Dr. Süleyman Akocak Adıyaman Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS (Q1) | ||
| Dergi ISSN | 0003-9861 Dergi Bilgileri (2025) | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 11-2025 |
| Cilt / Sayı / Sayfa | 773 / 0 / 110594–0 | DOI | 10.1016/j.abb.2025.110594 |
| Makale Linki | https://doi.org/10.1016/j.abb.2025.110594 | ||
| UAK Araştırma Alanları |
Tıbbi Biyokimya
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| Özet |
| The conformational and kinetic intricacies of enzyme-ligand interactions are critical for understanding molecular mechanisms underlying metabolic and neurodegenerative pathologies. Herein, we report a rationally designed series of ureido-benzenesulfonamides as dual-acting nanomolar inhibitors targeting aldose reductase (ALR2) and cholinesterases (AChE and BChE). Spectrophotometric inhibition assays revealed that compound 3SA-a displayed exceptional ALR2 affinity (KI = 7.00 ± 0.68 nM), surpassing epalrestat by over 30-fold. Likewise, 3SA-f selectively inhibited BChE with a KI of 24.20 ± 2.26 nM, outperforming tacrine by a factor of 7.8. Molecular docking simulations highlighted distinct dynamic binding modes: 3SA-a engaged ALR2’s catalytic cleft through a hydrogen bond with Tyr48 and water-bridged interactions, whereas 3SA-f leveraged π-π stacking and halogen bonding within BChE’s extended … |
| Anahtar Kelimeler |
| Ureido-benzenesulfonamides | Aldose reductase | Cholinesterase inhibition | Molecular docking | Structure-activity relationship |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 17 |
| Google Scholar | 21 |