Article ID Journal Published Year Pages File Type
1410588 Journal of Molecular Structure 2008 5 Pages PDF
Abstract

The interaction between irisflorentin (IFR) and bovine serum albumin (BSA) in physiological buffer (pH = 7.4) was investigated by fluorescence quenching technique and UV/vis absorption spectroscopy. The results of fluorescence titration revealed that IFR could strongly quench the intrinsic fluorescence of BSA through a dynamic quenching procedure. The apparent binding constants KA and number of binding sites n of IFR with BSA were obtained by fluorescence quenching method. The thermodynamic parameters, enthalpy change (ΔHθ) and entropy change (ΔSθ), were calculated to be 18.45 kJ mol−1 >0 and 149.72 J mol−1 K−1 >0, respectively, which indicated that the interaction of IFR with BSA was driven mainly by hydrophobic forces. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The distance r between donor (BSA) and acceptor (IFR) was calculated to be 3.88 nm based on Förster’s non-radiative energy transfer theory. The results of synchronous fluorescence spectra showed that binding of IFR with BSA can induce conformational changes in BSA.

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Physical Sciences and Engineering Chemistry Organic Chemistry
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