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Studying the interaction of bovine serum albumin with cefpirome sulfate by synchronous fluorescence spectroscopy

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


The interaction of cefpirome sulfate with bovine serum albumin in aqueous solution was studied by synchronous fluorescence and verified by fluorescence quenching spectroscopy. The data of synchronous fluorescence spectroscopy was used to infer the mechanism of the system and calculate the relevant parameters. The experimental results showed that the static mechanism played a role in the system; there was only one site for cefpirome sulfate on bovine serum albumin and the binding site was located in sub-domain IIA of BSA. Thermodynamic parameters were calculated, suggesting that hydrogen bond and hydrophobic interactions played a major role in stabilizing the complex. Based on the theory of ForesterÂ’s non-radiation energy transfer, binding distance is < 7 nm. In addition, synchronous fluorescence spectroscopy also provided information about the change of the molecular environment.


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索引于

  • 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
  • 研究期刊索引目录 (DRJI)
  • 秘密搜索引擎实验室
  • ICMJE

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