Chem. J. Chinese Universities

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Interaction Between PVA and BSA and Its Influence on the Conformation of BSA

WANG Gai-Zhen2, HE Jin-Tian1*, FENG Mei-Yan1, XIA Qing1   

    1. College of Life Science, Hebei Normal University, Shijiazhuang 050016, China;
    2. College of Environmental Science and Engineering, Hebei University of Science and Technology, Shijiazhuang 050018, China
  • Received:2008-04-23 Revised:1900-01-01 Online:2009-01-10 Published:2009-01-10
  • Contact: HE Jin-Tian

Abstract: Gel filtration chromatography, fluorescence spectrophotometry, differential scanning calorimetry(DSC) and Fourier transform infrared spectrophotometry(FTIR) were used to investigate the interaction between polyvinyl alcohol(PVA) and bovine serum albumin(BSA) under physiological conditions. The results show that BSA form complex with PVA. During BSA interaction with PVA, emission fluorescence derived from tryptophan of BSA was partially quenched upon binding to PVA. However, microenvironment of tryptophan was not changed during the binding process. The results of DSC suggest that the interaction of PVA with BSA maybe reduce the intramolecular interaction of BSA or PVA. FTIR spectrometry was combined with resolution enhancement technique Fourier deconvolution and Gaussian curve-fitting procedures to quantitate the spectral information from the amide Ⅰ bands of BSA within the freeze-dried mixture of PVA and BSA. The results show that the interaction of PVA with BSA affected only the β-sheet content but not α-helix, which is usually used as an indicator of the protein structural integrity in lyophilized state. Analysis of the BSA within the mixture of BSA and PVA suggest that interaction of PVA with the BSA maybe preserve the stability of BSA during lyophilization process.

Key words: Polyvinyl alcohol, Bovine serum albumin, Fourier transform infrared spectrometry, Gel chromatography, Fluorescence spectrometry

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