Rashad Al-Salahi1, Rohaya Ahmad2, ElHassane Anouar3, Nor Izzati Iwana Nor Azman2, Mohamed Marzouk3,4, Hatem A Abuelizz1. 1. Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, PO box 2457, Riyadh 11451, Saudi Arabia. 2. Faculty of Applied Sciences, Universiti Teknologi MARA, 40450 shah Alam, Selangor Darul Ehsan, Malaysia. 3. Department of Chemistry, College of Science & Humanities, Prince Sattam bin Abdulaziz University, PO Box 83, Al Kharj 11942, Saudi Arabia. 4. Chemistry of Natural Products Group, Center of Excellence for Advanced Sciences, National Research Centre, Dokki, Cairo 12622, Egypt.
Abstract
AIM: Using a simple modification on a previously reported synthetic route, 3-benzyl(phenethyl)-2-thioxobenzo[g]quinazolin-4(3H)-ones (1 and 2) were synthesized with high yields. Further transformation of 1 and 2 produced derivatives 3-26, which were structurally characterized based on NMR and MS data, and their in vitro α-glucosidase inhibitory activity was evaluated using Baker's yeast α-glucosidase enzyme. RESULTS: Compounds 2, 4, 8, 12 and 20 exhibited the highest activity (IC50 = 69.20, 59.60, 49.40, 50.20 and 83.20 μM, respectively) compared with the standard acarbose (IC50 = 143.54 μM). CONCLUSION: A new class of potent α-glucosidase inhibitors was identified, and the molecular docking predicted plausible binding interaction of the targets in the binding pocket of α-glucosidase and rationalized the structure-activity relationship (SARs) of the target compounds.
AIM: Using a simple modification on a previously reported synthetic route, 3-benzyl(phenethyl)-2-thioxobenzo[g]quinazolin-4(3H)-ones (1 and 2) were synthesized with high yields. Further transformation of 1 and 2 produced derivatives 3-26, which were structurally characterized based on NMR and MS data, and their in vitro α-glucosidase inhibitory activity was evaluated using Baker's yeast α-glucosidase enzyme. RESULTS: Compounds 2, 4, 8, 12 and 20 exhibited the highest activity (IC50 = 69.20, 59.60, 49.40, 50.20 and 83.20 μM, respectively) compared with the standard acarbose (IC50 = 143.54 μM). CONCLUSION: A new class of potent α-glucosidase inhibitors was identified, and the molecular docking predicted plausible binding interaction of the targets in the binding pocket of α-glucosidase and rationalized the structure-activity relationship (SARs) of the target compounds.
Authors: Rashad Al-Salahi; Moustapha E Moustapha; Hatem A Abuelizz; Abdulrahman I Alharthi; Khalid A Alburikan; Ismail T Ibrahim; Mohamed Marzouk; Mohamed A Motaleb Journal: Saudi Pharm J Date: 2018-06-06 Impact factor: 4.330
Authors: Hatem A Abuelizz; Hanem M Awad; Mohamed Marzouk; Fahd A Nasr; Ali S Alqahtani; Ahmed H Bakheit; Ahmed M Naglah; Rashad Al-Salahi Journal: RSC Adv Date: 2019-06-17 Impact factor: 4.036
Authors: Furqan Ahmad Saddique; Matloob Ahmad; Usman Ali Ashfaq; Muhammad Muddassar; Sadia Sultan; Magdi E A Zaki Journal: Pharmaceuticals (Basel) Date: 2022-01-17