Issue 2, 2011
From the journal:

Food & Function

Interaction of dietary flavonoids with gamma-globulin: molecular property-binding affinity relationship aspect

Fan Yang,a   Yaru Zhao,a   Guoyin Kaia  and  Jianbo Xiao*a  

* Corresponding authors

a Department of Biology, College of Life & Environment Science, Shanghai Normal University, 100 Guilin Rd, Shanghai, PR China
E-mail: jianboxiao@yahoo.com
Fax: +86 (021)64321291
Tel: +86 13611600163

Abstract

The molecular property-affinity relationship of dietary flavonoids for bovine gamma-globulin (γ-globulin) was investigated by fluorescence titration analysis. The quenching effects of flavonoids on γ-globulin fluorescence depended on the structures of flavonoids. The magnitudes of binding constants between flavonoids and γ-globulin were within the range of 103–105 L mol−1. These data were much smaller than the affinities between flavonoids and purified bovine and human serum albumins. The affinities of flavonoids for γ-globulin were strongly influenced by the structural differences of the compounds under study. The affinities for γ-globulin decreased with increasing partition coefficients and increased with increasing hydrogen bond acceptor numbers of flavonoids, which suggested that the binding interaction was mainly caused by hydrogen bond forces.

Graphical abstract: Interaction of dietary flavonoids with gamma-globulin: molecular property-binding affinity relationship aspect

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Article information

DOI
https://doi.org/10.1039/C0FO00092B
Article type
Paper
Submitted
22 Jul 2010
Accepted
13 Dec 2010
First published
12 Jan 2011

Food Funct., 2011,2, 137-141

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Interaction of dietary flavonoids with gamma-globulin: molecular property-binding affinity relationship aspect

F. Yang, Y. Zhao, G. Kai and J. Xiao, Food Funct., 2011, 2, 137 DOI: 10.1039/C0FO00092B

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