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• W2054657917 endingPage "9103" @default.
• W2054657917 startingPage "9092" @default.
• W2054657917 abstract "Flavonoids are structurally diverse and the most ubiquitous groups of dietary polyphenols distributed in various fruits and vegetables. In this study, the interaction between five flavonoids, namely formononetin-7-O-β-D-glucoside, calycosin- 7-O-β-D-glucoside, calycosin, rutin, and quercetin, and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorbance spectroscopy. In the discussion, it was proved that the fluorescence quenching of BSA by flavonoids was a result of the formation of a flavonoid-BSA complex. Fluorescence quenching constants were determined using the Stern-Volmer and Lineweaver-Burk equations to provide a measure of the binding affinity between the flavonoids and BSA. The binding constants ranked in the order quercetin>rutin>calycosin>calycosin-7-O-β-D-glucoside ≈ formononetin-7-O-β-D-glucoside. The results of thermodynamic parameters ΔG, ΔH, and ΔS at different temperatures indicated that the hydrophobic interaction played a major role in flavonoid-BSA association. The distance r between BSA and acceptor flavonoids was also obtained according to Förster's theory of non-radiative energy transfer." @default.
• W2054657917 created "2016-06-24" @default.
• W2054657917 creator A5007481575 @default.
• W2054657917 creator A5037388587 @default.
• W2054657917 creator A5054976089 @default.
• W2054657917 date "2010-12-09" @default.
• W2054657917 modified "2023-10-18" @default.
• W2054657917 title "Structural Relationship and Binding Mechanisms of Five Flavonoids with Bovine Serum Albumin" @default.
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• W2054657917 doi "https://doi.org/10.3390/molecules15129092" @default.
• W2054657917 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6259115" @default.
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