Abstract
The interaction of transresveratrol (TRES) with bovine serum albumin (BSA) has been investigated by ultraviolet‐visible, fluorescence, Fourier transform infrared spectroscopic methods and molecular modeling techniques. The fluorescence results show that the intrinsic fluorescence of BSA is quenched by TRES through a static quenching procedure. The binding constants of TRES with BSA at 292, 297 and 302 K are calculated as 10.22 × 104, 8.71 × 104, and 7.59 × 104 L mol−1, respectively, and corresponding numbers of binding sites are approximately equal to unity. The thermodynamic parameters ΔH and ΔS are estimated to be −21.82 kJ mol−1 and +21.15 J mol−1 K−1, which indicates that the interaction of TRES with BSA is driven mainly by hydrophobic forces and there are also hydrogen bonds and electrostatic interactions. The competitive experiments suggest that the binding site of TRES to BSA is probably located on site II. The results of infrared spectra show that the binding of TRES with BSA leads to conformational changes of BSA, and the binding stabilizes the α‐helix and β‐sheet at the cost of a corresponding loss in the β‐turn structure of BSA. The results of molecular modeling calculation clarify the binding mode and the binding sites which are in good accordance with the experiment results.
Highlights
Serum albumins, the major soluble protein constituents in the blood stream, bind and transport several exogenous and endogenous molecules like fatty acids, nutrients, steroids, and a large list of drugs
It is obvious that bovine serum albumin (BSA) has a strong fluorescence emission peak at about 347 nm, and the fluorescence intensity decreases gradually with increasing concentration of TRES, which indicates that TRES can interact with BSA and quench its intrinsic fluorescence
Interaction mechanism of TRES with BSA has been investigated by fluorescence spectroscopic, UV-vis spectroscopic, Fourier transform infrared (FTIR) spectroscopic methods and molecular modeling techniques
Summary
The major soluble protein constituents in the blood stream, bind and transport several exogenous and endogenous molecules like fatty acids, nutrients, steroids, and a large list of drugs. Bovine serum albumin (BSA) is an appropriate protein model for studying the interaction between serum albumins and drugs because of its medically important, unusual ligand-binding properties, low cost, availability, and structural homology with human serum albumin (HSA) [2, 3]. TRES has been shown to prevent or slow the progression of a wide variety of diseases, including cancer, cardiovascular disease, ischemic injuries, and Alzheimer’s disease [4,5,6,7,8] These properties accompanied with the lack of harmful effects make TRES attractive as a phytoalexin. The interaction of TRES with BSA has been investigated under imitated physiological conditions via spectroscopic methods and molecular modeling techniques. The molecular modeling was used to improve the understanding of the interaction of TRES with BSA
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