Yu Xianyong, Liao Zhixi, Jiang Bingfei, Hu Xiaolian, Li Xiaofang
Key Laboratory of Theoretical Organic Chemistry and Function Molecule, 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 200433, China.
Key Laboratory of Theoretical Organic Chemistry and Function Molecule, 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. 2015 Feb 25;137:129-36. doi: 10.1016/j.saa.2014.08.098. Epub 2014 Sep 3.
The interaction between novel spiro[cyclopropane-pyrrolizin] (NSCP) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy at 298 K, 304 K and 310 K under simulative physiological conditions. The results showed that NSCP can effectively quench the intrinsic fluorescence of BSA via static quenching. The binding constants, binding sites of NSCP with BSA were calculated. Hydrogen binds and van der Waals force played a major role in stabilizing the complex and the binding reaction were spontaneous. According to the Förster non-radiation energy transfer theory, the average binding distances between NSCP and BSA were obtained. What is more, the synchronous fluorescence spectra indicated that the conformation of BSA has been changed.
在模拟生理条件下，于298 K、304 K和310 K温度下，采用荧光光谱和紫外可见（UV-Vis）光谱法分析了新型螺环[环丙烷-吡咯嗪]（NSCP）与牛血清白蛋白（BSA）之间的相互作用。结果表明，NSCP可通过静态猝灭有效地猝灭BSA的固有荧光。计算了NSCP与BSA的结合常数和结合位点。氢键和范德华力在稳定复合物中起主要作用，且结合反应是自发的。根据Förster非辐射能量转移理论，获得了NSCP与BSA之间的平均结合距离。此外，同步荧光光谱表明BSA的构象发生了变化。
