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

Food & Function Pub Date: 2011-01-12 DOI: 10.1039/C0FO00092B

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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