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 C2C3 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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