Yu Xianyong, Liao Zhixi, Yao Qing, Liu Heting, Xie Wenlin
Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China; State Key Laboratory of Physical Chemistry of Solid Surfaces, Xiamen University, Xiamen 361005, China; Key Laboratory of Computational Physical Sciences, Fudan University, Ministry of Education, Shanghai, China.
Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2014 Jun 5;127:231-6. doi: 10.1016/j.saa.2014.02.064. Epub 2014 Feb 27.
The interaction between Phacolysin (PCL) and bovine serum albumin (BSA) under imitated physiological conditions was investigated by spectroscopic (fluorescence, UV-Vis absorption and Circular dichroism) techniques. The experiments were conducted at different temperatures (294K, 302K, 306K and 310K) and the results showed that the PCL caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant (Ka), binding sites (n) were obtained. The corresponding thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated at different temperatures. The results revealed that the binding process was spontaneous and the acting force between PCL and BSA were mainly hydrogen bonding and van der Waals forces. According to Förster non-radiation energy transfer theory, the binding distance between PCL and BSA was calculated to be 2.41nm. What is more, both synchronous fluorescence and Circular dichroism spectra confirmed the interaction, which indicated the conformational changes of BSA.
采用光谱技术（荧光、紫外-可见吸收和圆二色光谱）研究了在模拟生理条件下晶状体溶素（PCL）与牛血清白蛋白（BSA）之间的相互作用。实验在不同温度（294K、302K、306K和310K）下进行，结果表明PCL通过静态猝灭过程导致BSA的荧光猝灭。获得了结合常数（Ka）和结合位点（n）。计算了不同温度下相互作用体系的相应热力学参数（ΔH、ΔS和ΔG）。结果表明，结合过程是自发的，PCL与BSA之间的作用力主要是氢键和范德华力。根据Förster非辐射能量转移理论，计算出PCL与BSA之间的结合距离为2.41nm。此外，同步荧光光谱和圆二色光谱均证实了这种相互作用，这表明BSA的构象发生了变化。
