Interaction of Mixed Porphyrin-polypyridyl Ru(II) Complex with Bovine Serum Albumin  

作　　者：XU Lei LIU Ya-nan MEI Wen-jie HUANG Xiao-mei CHEN Tian-feng LIU Jie ZHENG Wen-jie 

机构地区：[1]Department of Chemistry, Jinan University, Guangzhou 510632, P. R. China [2]School of Pharmacy, Guangdong Pharmaceutical University, Guangzhou 510006, P. R. China

出　　处：《Chemical Research in Chinese Universities》2010年第5期693-698,共6页高等学校化学研究（英文版）

基　　金：Supported by the National Natural Science Foundation of China(Nos.20871056, 20771044 and 20901030);the Natural Science Foundation of Guangdong Province, China(Nos.8251063201000008 and 9451063201002077);the Planned Item of Science and Technology of Guangdong Province, China (No.2008A030201020);the "211" Project Grant of Jinan University,China

摘　　要：The interactions of mixed porphyrin-polypyridyl Ru（Ⅱ） complexes [m（Py-3＇）TPP-Ru（phen）2Cl]^＋（1） and its derivatives [Nim（Py-3＇）TPP-Ru（phen）2Cl]＋（2） and [Cum（Py-3＇）TPP-Ru（phen）2Cl]^＋（3）（phen=1,10-phenanthroline; m（Py-3＇）TPP=5-（3＇-pyridyl）-10,15,20-triphenylporphyrin） with bovine serum albumin（BSA） were investigated by fluorescence, UV-Vis and circular dichroism（CD） spectroscopies. The UV-Vis and CD spectral experiments indicated that the secondary structures of the protein were perturbed in the presence of the porphyrin Ru（Ⅱ） complex and the perturbation was enhanced under the irradiation with ultra-violet light. The fluorescence quenching mechanism of BSA by the three complexes was determined to be a static process, and the apparent binding constant K values for complexes 1, 2 and 3 measured by fluorescence quenching method were （3.86±0.03）×10^3 L/mol（n=0.94±0.04）, （5.69±0.04）× 103 L/mol（n=1.03±0.06）, and （6.54±0.02）× 10^3 L/mol（n=1.03±0.05）, respectively.The interactions of mixed porphyrin-polypyridyl Ru（Ⅱ） complexes [m（Py-3＇）TPP-Ru（phen）2Cl]^＋（1） and its derivatives [Nim（Py-3＇）TPP-Ru（phen）2Cl]＋（2） and [Cum（Py-3＇）TPP-Ru（phen）2Cl]^＋（3）（phen=1,10-phenanthroline; m（Py-3＇）TPP=5-（3＇-pyridyl）-10,15,20-triphenylporphyrin） with bovine serum albumin（BSA） were investigated by fluorescence, UV-Vis and circular dichroism（CD） spectroscopies. The UV-Vis and CD spectral experiments indicated that the secondary structures of the protein were perturbed in the presence of the porphyrin Ru（Ⅱ） complex and the perturbation was enhanced under the irradiation with ultra-violet light. The fluorescence quenching mechanism of BSA by the three complexes was determined to be a static process, and the apparent binding constant K values for complexes 1, 2 and 3 measured by fluorescence quenching method were （3.86±0.03）×10^3 L/mol（n=0.94±0.04）, （5.69±0.04）× 103 L/mol（n=1.03±0.06）, and （6.54±0.02）× 10^3 L/mol（n=1.03±0.05）, respectively.

关 键 词：PORPHYRIN Bovine serum albumin（BSA） Ru（Ⅱ） complex Binding 

分 类 号：O614.821[理学—无机化学] Q512.1[理学—化学]