Journal of Biomolecular Structure and Dynamics, ( ISI ), Volume (29), No (1), Year (2011-6) , Pages (181-206)

Title : ( Investigations with Spectroscopy, Zeta Potential and Molecular Modeling of the Non-Cooperative Behaviour Between Cyclophosphamide Hydrochloride and Aspirin upon Interaction with Human Serum Albumin: Binary and Ternary Systems from the View Point of Multi-Drug Therapy )

Authors: Zahra Omidvar , Kazem Parivar , Hamideh Sanee , Zeinab Amiri-Tehranizadeh , Ali Baratian , Mohammad Reza Saberi , Ahmad Asoodeh , Jamshidkhan Chamani ,

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The interaction between cyclophosphamide hydrochloride (CYC) and aspirin (ASA) with human serum albumin (HSA) was studied by various kind of spectroscopic, ζ potential and molecular modeling under physiological conditions. The fluorescence data showed that the binding of drugs to proteins caused strong static fluorescence quenching. The analysis of the fluorescence quenching of HSA in the binary and ternary systems displayed that ASA was affected by the complex formed between CYC and HSA. Moreover, CYC was influenced by the HSA-ASA complex. The inherent binding information, including the quenching mechanism, binding constants, number of binding sites, effective quenching constant, fraction of the initial fluorescence and thermodynamic parameters were measured by the fluorescence quenching technique at various temperatures. In addition, according to the synchronous fluorescence spectra of HSA, the results showed that the fluorescence quenching of HSA originated from the Trp and Tyr residues, and indicated a conformational change of HSA with the addition of the drugs. Far-UV CD spectra of HSA were recorded before and after the addition of ASA and CYC as binary and ternary systems. An increase in intensity of the positive CD peak of HSA was observed in the presence of the drugs. The results were interpreted by excited interactions between the aromatic residues of the HSA binding sites and the drugs bound to them. The distance r between donor and acceptor was obtained by the Förster energy according to fluorescence resonance energy transfer (FRET) and found to be 2.35 nm and 1.78 nm for CYC and ASA, respectively. This confirmed the existence of static quenching for proteins in the presence of CYC and ASA. Furthermore, docking studies pointed at a reduction of the affinity of each of the drug compounds to the protein in the presence of the other in meaningful amounts. Pre-binding of any of the said compounds forced the second to bind in a non-optimized location and orientation. The potential at the electrokinetic shear surface of the protein-drug solution were measured at several concentrations of the drugs by the ζ potential technique, which confirmed experimental and theoretical results.

Keywords

HSA; Fluorescence spectroscopic; Circular dichroism; Zeta potential; FRET; Molecular
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@article{paperid:1022207,
author = {Zahra Omidvar and Kazem Parivar and Hamideh Sanee and Zeinab Amiri-Tehranizadeh and Ali Baratian and Mohammad Reza Saberi and Asoodeh, Ahmad and Jamshidkhan Chamani},
title = {Investigations with Spectroscopy, Zeta Potential and Molecular Modeling of the Non-Cooperative Behaviour Between Cyclophosphamide Hydrochloride and Aspirin upon Interaction with Human Serum Albumin: Binary and Ternary Systems from the View Point of Multi-Drug Therapy},
journal = {Journal of Biomolecular Structure and Dynamics},
year = {2011},
volume = {29},
number = {1},
month = {June},
issn = {0739-1102},
pages = {181--206},
numpages = {25},
keywords = {HSA; Fluorescence spectroscopic; Circular dichroism; Zeta potential; FRET; Molecular modeling},
}

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%0 Journal Article
%T Investigations with Spectroscopy, Zeta Potential and Molecular Modeling of the Non-Cooperative Behaviour Between Cyclophosphamide Hydrochloride and Aspirin upon Interaction with Human Serum Albumin: Binary and Ternary Systems from the View Point of Multi-Drug Therapy
%A Zahra Omidvar
%A Kazem Parivar
%A Hamideh Sanee
%A Zeinab Amiri-Tehranizadeh
%A Ali Baratian
%A Mohammad Reza Saberi
%A Asoodeh, Ahmad
%A Jamshidkhan Chamani
%J Journal of Biomolecular Structure and Dynamics
%@ 0739-1102
%D 2011

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