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Food Res Int. 2017 Oct;100(Pt 1):226-233. doi: 10.1016/j.foodres.2017.07.010. Epub 2017 Jul 4.

Quercetin as a tyrosinase inhibitor: Inhibitory activity, conformational change and mechanism.

Author information

1
State Key Laboratory of Food Science and Technology, Nanchang University, 235 Nanjing East Road, Nanchang 330047, China.
2
State Key Laboratory of Food Science and Technology, Nanchang University, 235 Nanjing East Road, Nanchang 330047, China. Electronic address: gwzhang@ncu.edu.cn.
3
Institute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, 1801 Avenue of Zhongwu, Changzhou 213001, China.
4
State Key Laboratory of Food Science and Technology, Nanchang University, 235 Nanjing East Road, Nanchang 330047, China; New Zealand Institute of Natural Medicine Research, 8 Ha Crescent, Auckland 2104, New Zealand.

Abstract

Quercetin, a flavonoid compound, was found to inhibit both monophenolase and diphenolase activities of tyrosinase, and its inhibition against diphenolase activity was in a reversible and competitive manner with an IC50 value of (3.08±0.74)×10-5molL-1. Quercetin bound to tyrosinase driven by hydrophobic interaction, thereby resulted in a conformational change of tyrosinase and its intrinsic fluorescence quenching. Tyrosinase had one binding site for quercetin with the binding constant in the order of magnitude of 104Lmol-1. The molecular docking revealed that quercetin bound to the active site of tyrosinase and chelated a copper with the 3', 4'-dihydroxy groups. It can be deduced that the chelation may prevent the entrance of substrate and then inhibit the catalytic activity of tyrosinase. These findings may be helpful to understand the inhibition mechanism of quercetin on tyrosinase and functional research of quercetin in the treatment of pigmentation disorders.

KEYWORDS:

Inhibitory mechanism; Melanin; Molecular simulation; Quercetin; Tyrosinase

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