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Study of the Interaction between Trans-resveratrol and BSA by the Multi-spectroscopic Method

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Abstract

The interaction of trans-resveratrol and BSA was investigated by means of fluorescence quenching, resonance light scattering, ultraviolet spectroscopy and Fourier Transform Infrared Spectroscopy. Binding of trans-resveratrol to BSA quenches the BSA fluorescence and both static and dynamic quenching occur with complex formation. The apparent binding constants of trans-resveratrol and BSA at 20, 30 and 40 °C are 1.95×106, 1.70×106 and 1.65×106 L⋅mol−1, respectively. The binding site values are (1.25±0.02). According to the Förster theory of non-radiation energy transfer, the binding distances between trans-resveratrol and BSA are 3.47, 3.73 and 3.99 nm at 20, 30 and 40 °C, respectively. The negative enthalpy change and positive entropy change indicated that the interaction of trans-resveratrol and BSA was driven mainly by electrostatic forces. The process of binding was spontaneous whereby the Gibbs energy change was negative.

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Jiang, X.Y., Li, W.X. & Cao, H. Study of the Interaction between Trans-resveratrol and BSA by the Multi-spectroscopic Method. J Solution Chem 37, 1609–1623 (2008). https://doi.org/10.1007/s10953-008-9323-x

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  • DOI: https://doi.org/10.1007/s10953-008-9323-x

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