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

Mol Nutr Food Res. 2011 May:55 Suppl 1:S86-92. doi: 10.1002/mnfr.201000496. Epub 2011 Jan 10.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catechin / chemistry
  • Cattle
  • Flavonoids / chemistry*
  • Glycosylation
  • Hydrogenation
  • Hydroxylation
  • Molecular Structure
  • Phenols / chemistry*
  • Polyphenols
  • Protein Binding
  • Resveratrol
  • Spectrometry, Fluorescence
  • Stilbenes / chemistry
  • Structure-Activity Relationship
  • gamma-Globulins / chemistry*

Substances

  • Flavonoids
  • Phenols
  • Polyphenols
  • Stilbenes
  • gamma-Globulins
  • Catechin
  • Resveratrol