Tyrosinase and cholinesterase inhibitory activities and molecular docking studies on apigenin and vitexin

Background and Aims: Apigenin and viteksin are two phytochemical compounds in flavone structure. In this study, tyrosinase and cholinesterase inhibitory effects of apigenin and vitexin were tested. Then, molecular docking studies were conducted on these molecules. Methods: Cholinesterase inhibition was evaluated by minor modifications of Ellman's method and tyrosinase inhibition was evaluated by minor modifications of Masuda's method. Docking simulations were performed using the Schrodinger software suite. Results: When apigenin and vitexin were compared, apigenin showed higher inhibitory effect against butyrylcholinesterase (54[+ or -]1.7%) and tyrosinase (49.36[+ or -]0.24%), vitexin showed a higher inhibitory effect against acetylcholinesterase (66[+ or -]1.6%). Conclusion: When molecular interactions between tested compounds and inhibited enzymes were examined, it was observed that there were interactions especially between enzyme structures and benzopyran rings of these compounds and hydroxyl groups bound to these rings. Keywords: Apigenin, vitexin, enzyme inhibitory activity, molecular simulation