SCOPE: The aim of this study was to investigate the interaction between polyphenols and bovine ã-globulin.METHODS AND RESULTS: The relationship between the structural properties of natural polyphenols and their affinities for bovine ã-globulin were investigated by fluorescence titration analysis. Methylation of hydroxyl groups on flavonoids weakened the affinities for ã-globulin by 1.20-38.0 times. Hydroxylation on rings A, B, and C of flavonoids also significantly affected the affinity for ã-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 ã-globulin than non-galloylated and pyrogallol-type catechins. The glycosylation of resveratrol decreased its affinity for ã-globulin.CONCLUSION: The binding process with ã-globulin was strongly influenced by the structural differences of polyphenols.
Animals Catechin