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Spectral diagnostics of the interaction between pyridoxine hydrochloride and bovine serum albumin in vitro

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Abstract

The interaction between pyridoxine hydrochloride (VB6) and bovine serum albumin (BSA) were studied by spectroscopic methods including fluorescence spectroscopy and UV–visible absorption spectra. The quenching mechanism of fluorescence of BSA by VB6 was discussed. The number of binding sites n and observed binding constant K b was measured by fluorescence quenching method. The thermodynamic parameters ΔH θ, ΔG θ, ΔS θ at different temperatures were calculated and the results indicate the binding reaction is mainly entropy-driven and hydrophobic interaction played major role in the reaction. The distance r between donor (BSA) and acceptor (VB6) was obtained according to FÖrster theory of non-radiation energy transfer. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structural change of BSA molecules with addition of VB6, the result indicates that the secondary structure of BSA molecules is changed in the presence of VB6.

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Authors and Affiliations

  1. College of Chemical Engineering, Jingchu University of Technology, Jingmen, Hubei, 448000, P.R. China

    Huaxin Zhang & Min Zhang

  2. College of Chemistry, Central China Normal University, Wuhan, Hubei, 430027, P.R. China

    Xing Huang

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  1. Huaxin Zhang
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  2. Xing Huang
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  3. Min Zhang
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Correspondence to Huaxin Zhang.

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Zhang, H., Huang, X. & Zhang, M. Spectral diagnostics of the interaction between pyridoxine hydrochloride and bovine serum albumin in vitro. Mol Biol Rep 35, 699–705 (2008). https://doi.org/10.1007/s11033-007-9143-x

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  • DOI: https://doi.org/10.1007/s11033-007-9143-x

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