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Study on the Interaction of Matrine with Bovine Serum Albumin

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Abstract

The interaction of matrine (MAT) with bovine serum albumin (BSA) was studied via applying isothermal titration calorimetry, fluorescence and circular dichroism spectra. Important thermodynamic parameters were obtained based on the assumption that there were several classes of binding sites on the biomacromolecules and the supposition that the binding of the drug with the protein could be represented by the Langmuir absorption model. Analysis of the thermodynamic data revealed that there were two classes of binding sites on the biomacromolecules for the ligand molecules. This result was confirmed by the spectroscopic results.

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Authors and Affiliations

  1. College of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng, 252059, Shandong Province, P.R. China

    Xiangjun Sun, Xiangyu Xu, Min Liu, Linwei Li & Dezhi Sun

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  1. Xiangjun Sun
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  2. Xiangyu Xu
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  3. Min Liu
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  4. Linwei Li
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  5. Dezhi Sun
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Correspondence to Linwei Li.

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Sun, X., Xu, X., Liu, M. et al. Study on the Interaction of Matrine with Bovine Serum Albumin. J Solution Chem 39, 77–85 (2010). https://doi.org/10.1007/s10953-009-9487-z

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  • DOI: https://doi.org/10.1007/s10953-009-9487-z

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