Effect of luteolin on xanthine oxidase: Inhibition kinetics and interaction mechanism merging with docking simulation

被引：171

作者：

Yan, Jiakai ^{[1
]}

Zhang, Guowen ^{[1
]}

Hu, Yuting ^{[1
]}

Ma, Yadi ^{[1
]}

机构：

[1] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China

来源：

FOOD CHEMISTRY | 2013年 / 141卷 / 04期

基金：

中国国家自然科学基金;

关键词：

Luteolin; Xanthine oxidase; Inhibition kinetics; Fluorescence quenching; Circular dichroism; Molecular simulation; BOVINE SERUM-ALBUMIN; FLAVONOIDS; BINDING; ACID; ASSOCIATION; TYROSINASE; CELLS; GOUT;

D O I：

10.1016/j.foodchem.2013.06.092

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Xanthine oxidase (XO) catalyses hypoxanthine and xanthine to uric acid in human metabolism. Overproduction of uric acid will lead to hyperuricemia and finally cause gout and other diseases. Luteolin is one of the major components of celery and green peppers, its inhibitory activity on XO and their interaction mechanism were evaluated by multispectroscopic methods, coupled with molecular simulation. It was found that luteolin reversibly inhibited XO in a competitive manner with inhibition constant (K-i) value of (2.38 +/- 0.05) x 10(-6) mol l(-1). Luteolin could bind to XO at a single binding site and the binding was driven mainly by hydrophobic interactions. Analysis of synchronous fluorescence and circular dichroism spectra demonstrated that the microenvironment and secondary structure of XO were altered upon interaction with luteolin. The molecular docking results revealed luteolin actually interacted with the primary amino acid residues located within the active site pocket of XO. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：3766 / 3773

页数：8

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