Interaction between a potent corticosteroid drug - Dexamethasone with bovine serum albumin and human serum albumin: A fluorescence quenching and fourier transformation infrared spectroscopy study

被引:205
作者
Naik, P. N. [1 ]
Chimatadar, S. A. [1 ]
Nandibewoor, S. T. [1 ]
机构
[1] Karnatak Univ, PG Dept Studies Chem, Dharwad 580003, Karnataka, India
关键词
Bovine serum albumin; Human serum albumin; Dexamethasone; Fluorescence spectroscopy; FT-IR; Binding constant; ETHANOL OR/AND CAPTOPRIL; SECONDARY STRUCTURE; BINDING-SITES; AMIDE-I; PROTEINS; SPECTRA; PROBE;
D O I
10.1016/j.jphotobiol.2010.05.014
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This study was designed to examine the interaction of dexamethasone (DEX) with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with drug concentrations in the range of 2.5-20 mu M and BSA/HSA was fixed at 5.0 mu M. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of serum albumin by dexamethasone is static quenching mechanism. The binding sites number, n and binding constant, K were obtained at various temperatures. The distance r between dexamethasone and the protein was evaluated according to the theory of Foster energy transfer. The result of fluorescence spectra UV-vis absorption spectra and FT-IR spectra showed that the conformation of bovine serum albumin and human serum albumin has been changed in the presence of dexamethasone. The thermodynamic parameters, free energy change (Delta G(0)), enthalpy change (Delta H-0) and entropy change (Delta S-0) for BSA-DEX and HSA-DEX were calculated according to van't Hoff equation and discussed. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:147 / 159
页数:13
相关论文
共 43 条
[1]  
[Anonymous], 1996, MODERN QUANTUM CHEM
[2]   Resveratrol, Genistein, and Curcumin Bind Bovine Serum Albumin [J].
Bourassa, P. ;
Kanakis, C. D. ;
Tarantilis, P. ;
Pollissiou, M. G. ;
Tajmir-Riahi, H. A. .
JOURNAL OF PHYSICAL CHEMISTRY B, 2010, 114 (09) :3348-3354
[3]   Quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: From structure to spectrum [J].
Brauner, JW ;
Flach, CR ;
Mendelsohn, R .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (01) :100-109
[4]   An FTIR study of the structure of human serum albumin adsorbed to polysulfone [J].
Bummer, PM .
INTERNATIONAL JOURNAL OF PHARMACEUTICS, 1996, 132 (1-2) :143-151
[5]  
CARTER DC, 1994, ADV PROTEIN CHEM, V45, P153
[6]  
Chen G, 1990, Method of fluorescent analysis, P2
[7]   Probing the binding sites and the effect of berbamine on the structure of bovine serum albumin [J].
Cheng, Xiao-Xia ;
Lui, Yi ;
Zhou, Bo ;
Xiao, Xiao-He ;
Liu, Yi .
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, 2009, 72 (05) :922-928
[8]   Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin:: investigation by fluorescence spectroscopy [J].
Cui, FL ;
Fan, J ;
Li, JP ;
Hu, ZD .
BIOORGANIC & MEDICINAL CHEMISTRY, 2004, 12 (01) :151-157
[9]   Fluorescence spectroscopic study of serum albumin-bromadiolone interaction: fluorimetric determination of bromadiolone [J].
Deepa, S ;
Mishra, AK .
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS, 2005, 38 (03) :556-563
[10]   The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods [J].
Gao, H ;
Lei, LD ;
Liu, JQ ;
Kong, Q ;
Chen, XG ;
Hu, ZD .
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY, 2004, 167 (2-3) :213-221