NDLI: Separate and simultaneous binding effects through a non-cooperative behavior between cyclophosphamide hydrochloride and fluoxymesterone upon interaction with human serum albumin: multi-spectroscopic and molecular modeling approaches.

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Separate and simultaneous binding effects through a non-cooperative behavior between cyclophosphamide hydrochloride and fluoxymesterone upon interaction with human serum albumin: multi-spectroscopic and molecular modeling approaches.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Iranfar, Hediyeh Sanee, Hamideh Saberi, Mohammad Reza Chamani, Jamshidkhan Zohoorian-Abootorabi, Toktam
Description	Country affiliation: Iran Author Affiliation: Zohoorian-Abootorabi T ( Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran.)
Abstract	This study was designed to examine the interaction of two anti-breast cancer drugs, i.e., fluoxymesterone (FLU) and cyclophosphamide (CYC), with human serum albumin (HSA) using different kinds of spectroscopic, zeta potential and molecular modeling techniques under imitated physiological conditions. The RLS technique was utilized to investigate the effect of the two anticancer drugs on changes of the protein conformation, both separately and simultaneously. Our study suggested that the enhancement in RLS intensity was attributed to the formation of a new complex between the two drugs and the protein. Both drugs demonstrated a powerful ability to quench the fluorescence of HSA, and the fluorescence quenching action was much stronger when the two drugs coexisted. The quenching mechanism was suggested to be static as confirmed by time-resolved fluorescence spectroscopy results. The effect of both drugs on the conformation of HSA was analyzed using synchronous fluorescence spectroscopy. Our results revealed that the fluorescence quenching of HSA originated from the Trp and Tyr residues, and demonstrated a conformational change of HSA with the addition of both drugs. The binding distances between HSA and the drugs were estimated by the Förster theory, and it was revealed that nonradiative energy transfer from HSA to both drugs occurred with a high probability. According to CD measurements, the influence of both drugs on the secondary structure of HSA in aqueous solutions was also investigated and illustrated that the -helix content of HSA decreased with increasing drug concentration in both systems. Moreover, the zeta-potential experiments revealed that both drugs induced conformational changes on HSA. Docking studies were also performed and demonstrated that a reduction of the binding affinity between the drugs and HSA occurred in the presence of both drugs.
ISSN	13861425
Volume Number	88
e-ISSN	18733557
Journal	Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Language	English
Publisher	Elsevier
Publisher Date	2012-03-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cyclophosphamide Metabolism Fluoxymesterone Models, Molecular Serum Albumin Binding Sites Circular Dichroism Chemistry Energy Transfer Humans Hydrogen-ion Concentration Kinetics Light Molecular Conformation Protein Structure, Secondary Scattering, Radiation Spectrometry, Fluorescence Static Electricity Time Factors Tryptophan Journal Article Research Support, Non-u.s. Gov't Discipline Spectroscopy
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Atomic and Molecular Physics, and Optics Analytical Chemistry Instrumentation

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