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Investigation on the interaction of gliquidone to bovine serum albumin by fluorescence spectroscopy

Qiu-Ju Zhang, Bao-Sheng Liu, Gai-Xia Li, Rong Han


Gliquidone interacting with bovine serum albumin in physiological buffer (pH 7.4) was investigated by the fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy. The analysis of the quenching mechanism was done using Stern–Volmer plots which exhibit upward (positive) deviation. The experimental results indicated that the quenching mechanism between bovine serum albumin and gliquidone was static, and the electrostatic interaction played an important role in the interaction. In addition, binding sites n, the apparent binding constant Ka, the thermodynamic parameters andHillÂÂ’s coefficients were calculated at different temperatures. The results obtained fromthe synchronous fluorescence were same with the results from the fluorescence quenching spectroscopy. In addition, synchronous fluorescence spectroscopy provided information about conformational changes of proteins.


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  • 中国社会科学院
  • 谷歌学术
  • 打开 J 门
  • 中国知网(CNKI)
  • 引用因子
  • 宇宙IF
  • 电子期刊图书馆
  • 研究期刊索引目录 (DRJI)
  • 秘密搜索引擎实验室
  • ICMJE

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