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In Vitro Study of the Binding of Taxifolin to Bovine Serum Albumin and the Influence of Common Ions on the Binding

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Abstract

The interaction between taxifolin and bovine serum albumin (BSA), and the effects of some common ions on their interaction, were investigated by fluorescence and UV-visible absorption spectroscopy. The results indicate that taxifolin has a strong ability to quench the intrinsic fluorescence of BSA through a static quenching process. According to values of the thermodynamic parameters, the hydrophobic force plays a major role in the interaction. Based on Főster’s non-radiation theory, the energy transfer distances between BSA and taxifolin in the absence and presence of some common ions were obtained. The experimental results indicate that the transfer distances are almost unaffected by these ions. The conformation of BSA undergoes significant change from the formation of a taxifolin–BSA complex, which was studied by synchronous and three-dimensional fluorescence spectroscopy.

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Authors and Affiliations

  1. College of Chemistry, Jilin University, Chang Chun, 130012, China

    Xiaolei Shi, Xuwen Li, Yantao Sun, Wei Wei, Ruijie Yang, Hanqi Zhang & Yongri Jin

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  1. Xiaolei Shi
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  2. Xuwen Li
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  3. Yantao Sun
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  4. Wei Wei
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  5. Ruijie Yang
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  6. Hanqi Zhang
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  7. Yongri Jin
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Correspondence to Yongri Jin.

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Shi, X., Li, X., Sun, Y. et al. In Vitro Study of the Binding of Taxifolin to Bovine Serum Albumin and the Influence of Common Ions on the Binding. J Solution Chem 39, 482–494 (2010). https://doi.org/10.1007/s10953-010-9516-y

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  • DOI: https://doi.org/10.1007/s10953-010-9516-y

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