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

Year 2020, Volume: 50 Issue: 3, 268 - 271, 30.12.2020

Esen Sezen Karaoğlan Mehmet Koca

Abstract

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 Schrödinger software suite. 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 and hydroxyl groups bound to these rings.

Keywords

Apigenin, vitexin, enzyme inhibitory activity, molecular simulation

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