期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 122, 期 -, 页码 100-106出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2013.11.016
关键词
Venlafaxine hydrochloride; Bovine serum albumin; Protein-drug interaction; Multi-spectroscopy methods; Molecular docking; Binding mechanism
类别
资金
- Razi University Research Center
This study was designed to examine the interaction of racemic antidepressant drug S,R-venlafaxine hydrochloride (VEN) with bovine serum albumin (BSA) under physiological conditions. The mechanism of interaction was studied by spectroscopic techniques combination with molecular modeling. Stern-Volmer analysis of fluorescence quenching data shows the presence of the static quenching mechanism. The thermodynamic parameters indicated that the hydrogen bonding and weak van der Waals interactions are the predominant intermolecular forces stabilizing the complex. The number of binding sites (n) was calculated. Through the site marker competitive experiment, VEN was confirmed to be located in subdomain IIIA of BSA. The binding distance (r = 4.93 nm) between the donor BSA and acceptor VEN was obtained according to Forster's non-radiative energy transfer theory. According to UV-vis spectra and CD data binding of VEN leaded to conformational changes of BSA. Molecular docking simulations of S and R-VEN revealed that both isomers have similar interaction and the same binding sites, from this point of view S and R isomers are equal. (C) 2013 Elsevier B.V. All rights reserved.
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