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Chemistry and Industry of Forest Products ›› 2017, Vol. 37 ›› Issue (5): 79-87.doi: 10.3969/j.issn.0253-2417.2017.05.010

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Interactions Between Drugs and Bovine Serum Albumin in the Presence of Metal Ions by Spectral Methods

CAO Hongkun1, JIN Xiaowei2, ZHANG Enfeng1, YU Hui1, SHI Jingnan1, BIAN Hedong1,2   

  1. 1. School of Chemistry and Chemical Engineering, Guangxi University for Nationalities;Guangxi Key Laboratory of Chemistry and Engineering of Forest Products, Nan ning 530006, China;
    2. School of Chemistry and Phamaceutical Sciences, Guangxi Normal University;Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, Guilin 541004, China
  • Received:2017-02-22 Online:2017-10-25 Published:2017-10-30

Abstract: The mechanisms of the interaction between xanthotoxol(XAL) and bovine serum albumin(BSA) were investigated by fluorescence and circular dichroism(CD) spectrometry, as well as the effects of common metal ions(Fe3+, Cu2+, Zn2+, Cr3+) on the XAL-BSA binding. The quenching constants (kq) calculated by Stern-Volmer equation under 290,297 and 304 K were 6.316×1013,4.402×1013 and 3.554×1013 L/(mol·s), respectively. The result indicated that XAL could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was static quenching process. The binding constant (K) of XAL to BSA at 297 K was 3.47×105 L/mol. The addition of metal ions changed the binding constant. The distance between the tryptophan residues in BSA and XAL was 5.29 nm by using Föster's equation, and it decreased after interaction with metal ions. The CD spectrometry demonstrated that the secondary structure of BSA changed after its interaction with XAL, and α-helix content decreased; the secondary structure of BSA was also changed by addition of metal ions and α-helix content further reduced.

Key words: xanthotoxol, bovine serum albumin, interaction

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