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The interaction of dietary flavonoids with xanthine oxidase in vitro: molecular property-binding affinity relationship aspects

文献类型： 外文期刊

作者： Yuan, Mengmeng 1 ; Liu, Yi 1 ; Xiao, Aiping 1 ; Leng, Juan 1 ; Liao, Liping 1 ; Ma, Lei 1 ; Liu, Liangliang 1 ;

作者机构： 1.Chinese Acad Agr Sci, Inst Bast Fiber Crops, Changsha 410205, Hunan, Peoples R China; College of Chemistry and Chemical Engineering, Central South University, Changsha 410083, China

2.Zhengzhou Univ, State Key Lab Cotton Biol, Zhengzhou Res Base, Zhengzhou, Henan, Peoples R China.

3.Chinese Acad Agr Sci, Inst Bast Fiber Crops, Changsha 410205, Hunan, Peoples R China

期刊名称：RSC ADVANCES （ 影响因子：3.361； 五年影响因子：3.39 ）

ISSN： 2046-2069

年卷期： 2019 年 9 卷 19 期

页码：

收录情况： SCI

摘要： The molecular property-affinity relationships of dietary flavonoids binding to xanthine oxidase were investigated in vitro by comparing the binding constants obtained from a fluorescence-quenching method. The inhibitions of dietary flavonoids on xanthine oxidase were also investigated and analyzed, revealing that the binding process was influenced by the structural differences of the flavonoids under investigation. For example, methylation and hydroxylation at the 7- and 5-positions weakened the binding affinities, while hydroxylation at the 3- and 3-positions mostly improved binding affinities. Glycosylation and hydrogenation of the C-2?C-3 double bond also increased affinities for xanthine oxidase. In addition, galloylated catechins showed higher binding affinities than non-galloylated catechins. Trends in the binding affinities and inhibition of flavonoids during structure modifications were summarized. Affinities for xanthine oxidase and inhibition on xanthine oxidase changed in the opposite direction during the methylation and hydroxylation of flavonoids in the A ring, and the glycosylation and hydrogenation of C-2?C-3. However, affinities and inhibition for xanthine oxidase changed in the same direction during the methylation and hydroxylation of flavonoids in the B ring.

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