Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2011 Dec;83(1):609-13. doi: 10.1016/j.saa.2011.09.014. Epub 2011 Sep 16.
The fluorescence and ultraviolet spectroscopies were explored to study the interaction between N-confused porphyrins-edaravone diad (NCP-EDA) and bovine serum albumin (BSA) under simulative physiological condition at different temperatures. The experimental results show that the fluorescence quenching mechanism between NCP-EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites and the corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) of the interaction system were calculated at different temperatures. According to Förster non-radiation energy transfer theory, the binding distance between NCP-EDA and BSA was calculated to be 3.63 nm. In addition, the effect of NCP-EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.
荧光光谱法和紫外光谱法被用来研究在不同温度下模拟生理条件下，N-杂环卟啉-依达拉奉二联体（NCP-EDA）与牛血清白蛋白（BSA）之间的相互作用。实验结果表明，NCP-EDA 与 BSA 之间的荧光猝灭机制是一种联合猝灭（动态和静态猝灭）。在不同温度下计算了相互作用体系的结合常数、结合位点数和相应的热力学参数（ΔG、ΔH 和 ΔS）。根据福斯特非辐射能量转移理论，计算了 NCP-EDA 与 BSA 之间的结合距离为 3.63nm。此外，还利用同步荧光光谱法分析了 NCP-EDA 对 BSA 构象的影响。
