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Molecular structure-affinity relationship of natural polyphenols for bovine γ-globulin

✍ Scribed by Jianbo Xiao; Guoyin Kai; Fan Yang; Chunxi Liu; Xiaochen Xu; Koichiro Yamamoto

Book ID
102514963
Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
289 KB
Volume
55
Category
Article
ISSN
1613-4125

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✦ Synopsis

Abstract

Scope: The aim of this study was to investigate the interaction between polyphenols and bovine γ‐globulin.

Methods and results: The relationship between the structural properties of natural polyphenols and their affinities for bovine γ‐globulin were investigated by fluorescence titration analysis. Methylation of hydroxyl groups on flavonoids weakened the affinities for γ‐globulin by 1.20–38.0 times. Hydroxylation on rings A, B, and C of flavonoids also significantly affected the affinity for γ‐globulin. Glycosylation of flavonoids slightly affected the affinity depending on the conjugation site and the class of sugar moiety. Hydrogenation of the C2C3 double bond on flavonoids decreased the binding affinities. Galloylated catechins and catechol‐type catechins exhibited higher binding affinities for γ‐globulin than non‐galloylated and pyrogallol‐type catechins. The glycosylation of resveratrol decreased its affinity for γ‐globulin.

Conclusion: The binding process with γ‐globulin was strongly influenced by the structural differences of polyphenols.

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