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 

机构地区：[1]Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province,China West Normal University [2]Nanchong Petrochemical School

出　　处：《Journal of Pharmaceutical Analysis》2013年第4期257-269,共13页药物分析学报（英文版）

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

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.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.

关 键 词：Human serm albumin Bovine serum albumin Indigoiin Fluorescence spectro-scopy Binding constants 

分 类 号：O657.3[理学—分析化学]