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Inhibitory effects of four anthraquinones on tyrosinase activity: Insight from spectroscopic analysis and molecular docking.

Abstract：

:In this study, the inhibitory effects of four anthraquinones including chrysophanol, emodin, physcione and rhein on tyrosinase were investigated by enzyme inhibition assay. The results indicated that all of anthraquinones could significantly inhibit the activity of tyrosinase in a competitive manner. To gain insight into the inhibitory mechanism of anthraquinones on tyrosinase, spectroscopic analysis combined with molecular docking studies were performed. Fluorescence results showed that anthraquinones interacted with tyrosinase by static quenching in a molecular ratio of 1:1. Circular dichroism and molecular docking suggested that anthraquinones could not chelate directly the copper ions but they could bind to amino acid residues in the active site of tyrosinase via electrostatic forces and hydrophobic interactions, as well as hydrogen bonds, and the binding processes resulted in the conformational changes of tyrosinase and prevented the substrate (L-DOPA) from entering the active site, which led to the decrease of tyrosinase activity. Our study in this paper provides a scientific basis for revealing the inhibition of tyrosinase activity by anthraquinone compounds. As a natural inhibitor of tyrosinase, anthraquinones can be used as a potential agent to reduce enzymatic browning reactions, such as food browning and melanization of skin.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Zeng HJ,Sun DQ,Chu SH,Zhang JJ,Hu GZ,Yang R

doi

10.1016/j.ijbiomac.2020.05.193

subject

Has Abstract

pub_date

2020-10-01 00:00:00

pages

153-163

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)33355-9

journal_volume

160

pub_type

杂志文章

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