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Study of the Binding of Herbacetin to Bovine Serum Albumin by Fluorescence Spectroscopy

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Abstract

In this paper, the interaction between herbacetin and BSA was investigated by fluorescence and three-dimensional fluorescence spectroscopy under simulated physiological conditions. It was proved that the fluorescence quenching of BSA by herbacetin was mainly the result of the formation of a herbacetin–BSA complex. The modified Stern–Volmer quenching constant and the corresponding thermodynamic parameters ΔH 0, ΔG 0 and ΔS 0 were calculated at different temperatures. The results indicated that electrostatic interactions were the predominant intermolecular forces in stabilizing the complex. The distance r=3.23 nm between the donor (BSA) and acceptor (herbacetin) was obtained according to Förster’s nonradioactive energy transfer theory. The synchronous fluorescence and three-dimensional fluorescence spectra results showed that the hydrophobity of amino acid residues increased in the presence of herbacetin. These results revealed that the microenvironment and conformation of BSA changed during the binding reaction.

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Authors and Affiliations

  1. College of Chemistry and Chemical Engineering, Mianyang Normal University, Mianyang, 621000, P.R. China

    Shuya Cui & Xiaoli Hu

  2. School of Physics and Chemistry, Xihua University, Chengdu, 6100039, P.R. China

    Jiaqin Liu

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  1. Shuya Cui
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  2. Xiaoli Hu
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  3. Jiaqin Liu
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Correspondence to Xiaoli Hu.

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Cui, S., Hu, X. & Liu, J. Study of the Binding of Herbacetin to Bovine Serum Albumin by Fluorescence Spectroscopy. J Solution Chem 40, 764–774 (2011). https://doi.org/10.1007/s10953-011-9684-4

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  • DOI: https://doi.org/10.1007/s10953-011-9684-4

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