Akademik Veri Yönetim Sistemi
Russian Journal of Bioorganic Chemistry, cilt.50, sa.1, ss.191-200, 2024 (SCI-Expanded)
Abstract: Objective: It is aimed to synthesize new amino acid-conjugated coumarin-benzotriazole molecules and to investigate their acetylcholinesterase, urease, and lipase inhibition properties. Methods: Urease inhibitory activities of new compounds and standard were determined spectrophotometrically according to the method of Van Slykeand Archibald. The lipase activity assay was determined using the method of Bendicho. The acetylcholinesterase enzymatic activity was measured according to the method described by Ingkaninan. Results and Discussion: All synthesized compounds showed effective urease, lipase, and acetylcholinesterase inhibitory activities. Compound (Vd) has the most potent enzyme inhibition activity against urease with an IC50 = 0.038 ± 0.022 μM. Compound (Vc) has the most potent enzyme inhibition activity against lipase with an IC50 = 0.101 ± 0.046 μM. Compound (Ve) has the best inhibitory effect against acetylcholinesterase enzyme with an IC50 = 0.003 ± 0.001 μM. Conclusions: A novel series of coumarin-amino acid-benzotriazole conjugates have been synthesized, and their urease, lipase, and acetylcholinesterase (AChE) inhibitor activities were determined. Most of the tested compounds showed higher urease inhibitory activity IC50 values ranging from 0.038 ± 0.022 to 0.086 ± 0.057 µM than thiourea. Among the series, compound (Vc) proved to be the most potent showing lipase inhibitory activity with an IC50 = 0.101 ± 0.046 μM when compared to the standard inhibitor Orlistat with an IC50 = 0.185 ± 0.075 μM. Compounds (Ve), (VIa), (VId), and (VIe) were found to exhibit potent inhibitory properties against acetylcholinesterase enzyme in the range of IC50 = 0.003 ± 0.001–0.010 ± 0.006 μM when compared to the tacrine as standard (IC50 = 0.029 ± 0.012 μM).