Analysis of Binding Interaction between Captopril and Human Serum Albumin英文文献资料.docVIP

American Journal of Analytical Chemistry, 2011, 2, 250-257 doi:10.4236/ajac.2011.22030 Published Online May 2011 (http://www.SciRP.org/journal/ajac) Analysis of Binding Interaction between Captopril and Human Serum Albumin Xiaoyan Gao, Yingcai Tang, Wanqi Rong, Xiaoping Zhang, Wujie Zhao, Yanqin Zi Department of Chemistry and Materials Science, Huaibei Normal University, Huaibei, China E-mail: ziyanqin@163.com Received October 8, 2010; revised January 24, 2011; accepted May 10, 2011 Abstract The interaction between captopril, an inhibitor of angiotensin converting enzyme and human serum albumin, a principal plasma protein in the liver has been investigated in vitro under a simulated physiological condi- tion by UV-vis spectrophotometry and fluorescence spectrometry. The intrinsic fluorescence intensity of human serum albumin was strongly quenched by captopril. The binding constants and the number of binding sites can be calculated from the data obtained from fluorescence quenching experiments. The negative value of ?G reveals that the binding process is a spontaneous process. According to the van’t Hoff equation, the 0 standard enthalpy change (?H 0 0 35.98 KJ?mol and 221.25 J ?mol ) and standard entropy change (?S ) for the reaction were calculated to be –1 –1 K. It indicated that the hydrophobic interactions play a main role in the binding of captopril to human serum albumin. In addition, the distance between captopril (acceptor) and tryptophan residues of human serum albumin (donor) was estimated to be 1.05 nm according to the F?rster’s resonance energy transfer theory. The results obtained herein will be of biological significance in pharma- cology and clinical medicine. Keywords: Human Serum Albumin, Captopril, Fluorescence Quenching, Stern-Volmer Equation, The F?rster’s Resonance Energy Transfer Theory 1. Introduction acti