Abstract
In this paper, the interaction between flavonol p-coumaroylglucoside tiliroside and BSA was investigated by fluorescence quenching spectra, synchronous fluorescence spectra, and three-dimensional fluorescence spectra under simulative physiological conditions. It was proved that the fluorescence quenching of BSA by tiliroside was mainly a result of the formation of a tiliroside–BSA complex. The modified Stern-Volmer quenching constant and the corresponding thermodynamic parameters Δ H, Δ G and Δ S at different temperatures were calculated. The results indicated that electrostatic interactions were the predominant intermolecular forces in stabilizing the complex. The distance r = 3.95 nm between the donor (BSA) and acceptor (tiliroside) was obtained according to Förster's nonradioactive energy transfer theory. The synchronous fluorescence and three-dimensional fluorescence spectra results showed the microenvironment and conformation of BSA were changed in the binding reaction.
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