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      Spectroscopic investigation of interaction between mangiferin and bovine serum albumin

      , , , ,
      Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
      Elsevier BV

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          Abstract

          The mechanism of interaction between mangiferin (MA) and bovine serum albumin (BSA) in aqueous solution was investigated by fluorescence spectra, synchronous fluorescence spectra, absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy. The binding constants and binding sites of MA to BSA at different reaction times were calculated. And the distance between MA and BSA was estimated to be 5.20 nm based on Föster's theory. In addition, synchronous fluorescence and FT-IR measurements revealed that the secondary structures of the protein changed after the interaction of MA with BSA. As a conclusion, the interaction between the anti-diabetes Chinese medicine MA and BSA may provide some significant information for the mechanism of the traditional chinese medicine MA on the protein level to cure diabetes or other diseases.

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          Author and article information

          Journal
          Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
          Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
          Elsevier BV
          13861425
          September 2009
          September 2009
          : 73
          : 5
          : 936-941
          Article
          10.1016/j.saa.2009.04.025
          19501542
          6b153660-8568-4aa8-bb68-e5b5310a3c4c
          © 2009

          https://www.elsevier.com/tdm/userlicense/1.0/

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