Mechanistic investigation of anthocyanidin derivatives as α-glucosidase inhibitors |
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| Institution: | 1. Department of Chemistry Tehran North Branch, Islamic Azad University, Tehran, Iran;2. Cellular and Molecular Biology Research Center, Health Research Institute, Babol University of Medical Sciences, Babol, Iran;3. Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran;4. Department of Medicinal Chemistry, Faculty of Pharmacy and Pharmaceutical Sciences, Research Center, Tehran University of Medical Sciences, Tehran, Iran;5. Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran;6. CinnaGen Medical Biotechnology Research Center, Alborz University of Medical Sciences, Karaj, Iran;7. Nano Alvand Company, Avicenna Tech Park, Tehran University of Medical Sciences, Tehran 1439955991, Iran;1. Cellular and Molecular Biology Research Center, Health Research Institute, Babol University of Medical Sciences, Babol, Iran;2. Department of Chemistry, Shiraz University of Technology, Shiraz, Iran;3. Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Iran;4. School of Chemistry, College of Science, University of Tehran, Tehran, Iran;5. Department of Biotechnology, Iranian Research Organization for Science and Technology (IROST), Tehran, Iran;6. Diabetes Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran;7. Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran;1. Jiangxi Key Laboratory of Natural Product and Functional Food, College of Food Science and Engineering Jiangxi Agricultural University, Nanchang 33045, China;2. Library of Jiangxi Agricultural University, Nanchang 330045, China;1. Department of Biotechnology, Goa University, Taleigao Plateau, Goa 403 206, India;2. Department of Chemistry, Goa University, Taleigao Plateau, Goa 403 206, India;3. Organic Chemistry Department, RUDN University, 6 Miklukho-Maklay Street, Moscow 117198, Russian Federation;1. College of Biological and Chemical Engineering, Anhui Polytechnic University, Wuhu 241000, PR China;2. Affiliated Hospital of Shandong University of Traditional Chinese Medicine, Jinan 250011, PR China;3. College of Pharmacy, Shandong University of Traditional Chinese Medicine, Jinan 250355, PR China |
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| Abstract: | Eight anthocyanidin derivatives (1–8) were evaluated as potential inhibitors of the catalysis of α-glucosidase. Among them, compounds 4 and 8 had the highest levels of inhibitory activity at 100 μM (IC50 values of 14.4 ± 0.1 and 29.7 ± 1.2 μM) and acted in a dose-dependent manner. Enzyme kinetic analysis further revealed that these inhibitors interacted with α-glucosidase in a mixed noncompetitive mode. Moreover, fluorescence quenching studies provided parameters for calculating the binding mechanism between receptor and ligand. On the basis of these studies, and in silico simulations, we determined that the ligand was likely docked in the receptor. Thus, compounds 4 and 8 are excellent potential targets for in vitro cell-based and in vivo assays related to treatment of diabetes. |
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| Keywords: | Anthocyanidin derivative α-Glucosidase Mixed noncompetitive mode |
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