Inhibitory mechanism of xanthine oxidase activity by caffeoylquinic acids in vitro

被引：40

作者：

Wan, Yin ^{[1
,2
]}

Qian, Jin ^{[1
,2
]}

Li, Yizhen ^{[1
,2
]}

Shen, Yuefeng ^{[1
,2
]}

Chen, Yanru ^{[1
,2
]}

Fu, Guiming ^{[1
,2
]}

Xie, Mingyong ^{[1
,2
]}

机构：

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

[2] Nanchang Univ, Coll Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2021年 / 184卷

基金：

中国国家自然科学基金;

关键词：

Caffeoylquinic acids; Xanthine oxidase; Inhibitory mechanism; SPECTROSCOPY; FLAVONOIDS; GALANGIN; KINETICS; INSIGHTS; PROTEIN; LEAVES;

D O I：

10.1016/j.ijbiomac.2021.06.075

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

In this study, the inhibitory activities of eight caffeoylquinic acids (CQAs) against xanthine oxidase (XOD) in vitro were investigated, and the interaction mechanisms between each compound and XOD were studied. HPLC and fluorescence spectra showed that the inhibitory activities of dicaffeoylquinic acids (diCQAs) were higher than that of monocaffeoylquinic acids (monoCQAs), due to the main roles of hydrophobic interaction and hydrogen bond between XOD and diCQAs. Both the binding constant and the lowest binding energy data indicated that the affinities of diCQAs to XOD were stronger than that of monoCQAs. Circular dichroism showed that the structure of XOD was compacted with the increased of alpha-helix content, resulting in decreased enzyme catalytic activity. Molecular docking revealed that CQAs preferentially bind to the flavin adenine dinucleotide region in XOD. These results provided the mechanisms of CQAs on inhibiting XOD and the further utilization of CQAs as XOD inhibitors to prevent hyperuricemia.

引用

页码：843 / 856

页数：14

共 43 条

[1]

Insights from multispectral and molecular docking investigation on the xanthine oxidase inhibition by 1,4-dicaffeoylquinic acid [J].