title: Interaction of dietary flavonoids with gamma-globulin: molecular property-binding affinity relationship aspect.
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 10(3)-10(5) 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.
authors.affiliation: Department of Biology, College of Life & Environment Science, Shanghai Normal University, 100 Guilin Rd, Shanghai 200234, PR China.
authors.forename: Fan
authors.initials: F
authors.lastname: Yang
authors.forename: Yaru
authors.initials: Y
authors.lastname: Zhao
authors.forename: Guoyin
authors.initials: G
authors.lastname: Kai
authors.forename: Jianbo
authors.initials: J
authors.lastname: Xiao
mesh_terms: D000818:Animals; D002417:Cattle; D005419:Flavonoids / Q000097:blood* / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D008956:Models, Chemical; D011485:Protein Binding / Q000502:physiology; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods; D013329:Structure-Activity Relationship; D005719:gamma-Globulins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D005419:Flavonoids; D012709:Serum Albumin; D005719:gamma-Globulins