School of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Mar;88:130-6. doi: 10.1016/j.saa.2011.12.017. Epub 2011 Dec 22.
The interaction of cationic pyridinium porphyrins appending methylpyridyl, hydroxyphenyl, propionoxyphenyl or carboxyphenyl group at meso-20-position of porphyrin core with bovine serum albumin (BSA), was studied by the combination of absorption spectroscopy, surface-enhanced Raman spectroscopy (SERS), circular dichroism (CD) spectroscopy, fluorescence spectroscopy and synchronous spectroscopy. The spectral monitoring results indicate that the studied compounds could bind with the BSA molecule and the calculated binding constants show that the tetracationic porphyrin has higher binding affinity than those tricationic ones. The interactions between porphyrins and BSA employ an electrostatic binding mechanism and there was only one binding site which located on the surface of the protein molecule.
通过吸收光谱、表面增强拉曼光谱（SERS）、圆二色性（CD）光谱、荧光光谱和同步光谱的结合，研究了在卟啉核心的meso-20-位上附加甲基吡啶基、羟基苯基、丙氧羰基苯基或羧基苯基的阳离子吡啶卟啉与牛血清白蛋白（BSA）的相互作用。光谱监测结果表明，所研究的化合物可以与 BSA 分子结合，并且计算出的结合常数表明四阳离子卟啉比三阳离子卟啉具有更高的结合亲和力。卟啉与 BSA 之间的相互作用采用静电结合机制，并且只有一个结合位点位于蛋白质分子的表面。
