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The investigation of the interaction between ribavirin and bovine serum albumin by spectroscopic methods

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Abstract

The interaction between ribavirin (RIB) with bovine serum albumin (BSA) has been investigated by fluorescence quenching technique in combination with UV–vis absorption and circular dichroism (CD) spectroscopies under the simulative physiological conditions. The quenching of BSA fluorescence by RIB was found to be a result of the formation of RIB–BSA complex. The binding constants and the number of binding sites were calculated at three different temperatures. The values of thermodynamic parameters ∆H, ∆S, ∆G at different temperatures indicate that hydrophobic and hydrogen bonds played important roles for RIB–BSA association. The binding distance r was obtained according to the theory of FÖrster’s non–radiation energy transfer. The displacement experiments was performed for identifying the location of the binding site of RIB on BSA. The effects of common ions on the binding constant of RIB and BSA were also examined. Finally, the conformational changes of BSA in the presence of RIB were also analyzed by CD spectra and Synchronous fluorescence spectra.

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Acknowledgment

We gratefully acknowledge financial support of Liaoning Natural Science Foundation (Grant no: 20102087).

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Authors and Affiliations

  1. College of Chemistry, Liaoning University, Shenyang, 110036, People’s Republic of China

    Xing-Jia Guo, Xiao-Wei Han, Ping-Li Kang, Yu-Chun Jiang & Xiang-Jun Zhang

  2. School of Pharmaceutical Science, Liaoning University, Shenyang, 110036, People’s Republic of China

    Ai-Jun Hao

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  1. Xing-Jia Guo
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Correspondence to Xing-Jia Guo.

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Guo, XJ., Hao, AJ., Han, XW. et al. The investigation of the interaction between ribavirin and bovine serum albumin by spectroscopic methods. Mol Biol Rep 38, 4185–4192 (2011). https://doi.org/10.1007/s11033-010-0539-7

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  • DOI: https://doi.org/10.1007/s11033-010-0539-7

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