Characterization of interaction and the effect of carbamazepine on the structure of human serum albumin

被引：83

作者：

Kalanur, Shankara S. ^{[1
]}

Seetharamappa, J. ^{[1
]}

Kalalbandi, Veerendra Kumar A. ^{[1
]}

机构：

[1] Karnatak Univ, Dept Chem, Dharwad 580003, Karnataka, India

来源：

JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS | 2010年 / 53卷 / 03期

关键词：

Carbamazepine; Human serum albumin; Spectroscopic and voltammetric approach; Hydrophobic interactions; Site I of subdomain IIA; FLUORESCENCE SPECTROSCOPY; CHROMATOGRAPHIC ANALYSIS; BINDING;

D O I：

10.1016/j.jpba.2010.05.025

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The binding of carbamazepine (CBZ) to human serum albumin (HSA) was investigated under simulative physiological conditions In this study, intrinsic fluorescence of tryptophan-214 in HSA was monitored upon the addition of CBZ Binding constant of CBZ-HSA was calculated by the remarkable static quenching effect of CBZ and found to be (2.081 +/- 0 023) x 10(4) M-1. The fluorimetric results revealed that the hydrophobic interaction was a predominant Intermolecular force for stabilizing the complex, which is also in agreement with the results obtained from voltammetric approach Three site probes, warfarin. Ibuprofen and digitoxin, were employed in fluorescence displacement experiments to locate the exact binding site for CBZ in HSA The alteration in secondary structure of protein in the presence of CBZ was confirmed by the evidences from circular dichroism and FT-IR spectroscopy Further, the distance r between donor (Trp-214) and acceptor (CBZ) was obtained according to fluorescence resonance energy transfer (FRET) (C) 2010 Elsevier B V All rights reserved

引用

页码：660 / 666

页数：7

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