利用光谱法研究三氯生与牛血清白蛋白的相互作用。
Investigation on the interaction between triclosan and bovine serum albumin by spectroscopic methods.
机构信息
Department of Chemistry, College of Sciences, Northeastern University, Shenyang, P.R. China.
College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, P.R. China.
出版信息
J Environ Sci Health B. 2020;55(1):52-59. doi: 10.1080/03601234.2019.1656499. Epub 2019 Aug 27.
Multi-spectroscopic and molecular docking methods were used to study the interaction between triclosan (TCS) and bovine serum albumin (BSA). The results indicated that the fluorescence quenching of BSA by TCS was due to the formation of TCS-BSA complex through static quenching. This result was also demonstrated by time-resolved fluorescence experiment. The binding constants and number of binding sites between TCS and BSA were 1.30 × 10 M and 1.17 at 298 K, respectively. The thermodynamic parameters were studied in detail which suggested that hydrophobic forces and hydrogen bond played major roles in the TCS-BSA interaction. Moreover, the site marker competitive experiments and docking studies revealed that TCS could bind BSA into site I in subdomain IIA. All the results of UV-vis spectrophotometry, circular dichroism spectroscopy and synchronous fluorescence spectroscopy showed that interaction between TCS and BSA induced conformation changes of BSA.
采用多光谱和分子对接方法研究了三氯生（TCS）与牛血清白蛋白（BSA）之间的相互作用。结果表明，TCS 对 BSA 的荧光猝灭是由于通过静态猝灭形成了 TCS-BSA 复合物。这一结果也通过时间分辨荧光实验得到了证明。在 298 K 时，TCS 与 BSA 之间的结合常数和结合位点数分别为 1.30×10^4 M 和 1.17。详细研究了热力学参数，结果表明疏水作用力和氢键在 TCS-BSA 相互作用中起主要作用。此外，位点标记竞争实验和对接研究表明，TCS 可以将 BSA 结合到亚结构域 IIA 的位点 I 中。紫外可见分光光度法、圆二色光谱法和同步荧光光谱法的所有结果均表明，TCS 与 BSA 之间的相互作用导致 BSA 构象发生变化。
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