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

Abstract

Background and Aims: Apigenin and viteksin are two phytochemical compounds in flavone structure. In this study, tyrosinaseand cholinesterase inhibitory effects of apigenin and vitexin were tested. Then, molecular docking studies were conductedon these molecules.Methods: Cholinesterase inhibition was evaluated by minor modifications of Ellman’s method and tyrosinase inhibition wasevaluated by minor modifications of Masuda’s method. Docking simulations were performed using the Schrödinger softwaresuite.Results: When apigenin and vitexin were compared, apigenin showed higher inhibitory effect against butyrylcholinesterase(54±1.7%) and tyrosinase (49.36±0.24%), vitexin showed a higher inhibitory effect against acetylcholinesterase (66±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 andhydroxyl groups bound to these rings.