Journal
MOLECULES
Volume 15, Issue 12, Pages 9092-9103Publisher
MDPI
DOI: 10.3390/molecules15129092
Keywords
flavonoids; bovine serum albumin; fluorescence quenching; binding mechanism
Funding
- Program for Changjiang Scholars and Innovative Research Team in University [IRT0868]
- National Science and Technology Major Project 'Creation of Major New Drugs' from China [2009ZX09502-020]
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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-beta-D-glucoside, calycosin-7-O-beta-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-beta-D-glucoside approximate to formononetin-7-O-beta-D-glucoside. The results of thermodynamic parameters Delta G, Delta H, and Delta S 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 Forster's theory of non-radiative energy transfer.
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