Study of the interaction between doxepin hydrochloride and bovine serum albumin by spectroscopic techniques

被引：76

作者：

Kandagal, P. B. ^{[1
]}

Seetharamappa, J. ^{[1
]}

Ashoka, S. ^{[1
]}

Shaikh, S. M. T. ^{[1
]}

Manjunatha, D. H. ^{[1
]}

机构：

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

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2006年 / 39卷 / 4-5期

关键词：

bovine serum albumin; doxepin hydrochloride; spectroscopic techniques; fluorescence resonance energy transfer;

D O I：

10.1016/j.ijbiomac.2006.03.027

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：

The binding of doxepin hydrochloride (DH) to bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, UV-vis absorption and circular dichroism) techniques. The binding parameters have been evaluated by fluorescence quenching method. The thermodynamic parameters, Delta H degrees, Delta S degrees and Delta G degrees calculated at different temperatures indicated that the hydrogen bond and hydrophobic forces played a major role in the interaction of DH with BSA. Based on the Forster's theory of non-radiation energy transfer, the binding average distance, r between the donor (BSA) and acceptor (DH) was evaluated and found to be 2.7 nm. Spectral results observed showed that the binding of DH to BSA induced conformational changes in BSA. The effect of common ions on the binding of DH to BSA was also examined. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：234 / 239

页数：6

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