Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches

作     者：Zheng-Jun Cheng Hong-Mei Zhao Qian-Yong Xu Rong Liu 

作者机构：Chemical Synthesis and Pollution Control Key Laboratory of Sichuan ProvinceChina West Normal University Nanchong Petrochemical School 

出 版 物：《Journal of Pharmaceutical Analysis》 (药物分析学报（英文版）)

年 卷 期：2013年第3卷第4期

页      面：257-269页

学科分类：0710[理学-生物学] 1007[医学-药学(可授医学、理学学位)] 1002[医学-临床医学] 081704[工学-应用化学] 07[理学] 0817[工学-化学工程与技术] 08[工学] 070302[理学-分析化学] 0703[理学-化学] 0702[理学-物理学] 

基　　金：support by the Education Department of Sichuan Province (12ZA171) 

主　　题：Human serm albumin Bovine serum albumin Indigoiin Fluorescence spectro-scopy Binding constants 

摘      要：The binding characteristics of indigotin with human serum albumin （HSA） and bovine serum albumin （BSA） have been investigated by various spectroscopic techniques. Spectroscopic analysis revealed that the quenching mechanism between indigotin and HSA/BSA belonged to the static quenching. The displacement experiments suggested that indigotin primarily bound to tryptophan residues on proteins within site I. The thermodynamic parameters indicated that the binding of indigoti^HSA/BSA mainly depended on the hydrophobic interaction. The binding distance of indigotin to HSA/BSA was evaluated. The results by synchronous fluorescence, three- dimensional fluorescence, Fourier Transform Infrared spectroscopy （FT-IR） and circular dichroism （CD） spectra showed that the conformation of proteins altered in the presence of indigotin.