Repository of Research and Investigative Information

Repository of Research and Investigative Information

Baqiyatallah University of Medical Sciences

Multispectral and molecular docking studies on the interaction of human serum albumin with iohexol

(2017) Multispectral and molecular docking studies on the interaction of human serum albumin with iohexol. Journal of Molecular Liquids. pp. 459-467. ISSN 0167-7322

Full text not available from this repository.

Official URL: http://apps.webofknowledge.com/InboundService.do?F...

Abstract

Interaction between iohexol and human serum albumin (HSA) was studied by using some spectroscopic and molecular docking methods at different temperatures (298, 303, 310 and 318 K) under physiological pH. Fluorescence quenching was the result of the collision between fluorophore and the iohexol and dynamic quenching mechanism was dominant. The binding constant (K similar to 10(3)) and the number of binding sites (n similar to 1) were also obtained from fluorescence titration data. The thermodynamic parameters namely enthalpy change (Delta H), Gibbs free energy change (Delta G), and entropy change (Delta S) were calculated and the results suggested that hydrophobic interaction was the significant intermolecular force between HSA and iohexol. FT-IR analyses showed that interaction iohexol with HSA caused a conformational change of the protein. The CD spectra revealed major alterations in the secondary structure of HSA with increase of alpha-helices, content and reduction of beta-turn. Binding distance between iohexol and HSA was calculated by the Forster Resonance Energy Transfer (FRET) method. The site marker competitive experiments suggested that the binding site of iohexol and HSA was probably located on sites I and II. Results determined by molecular docking method were in agreement with thermodynamic and spectroscopic data and confirmed the binding mechanism of iohexol to HSA. (C) 2017 Published by Elsevier B.V.

Item Type: Article
Keywords: Dynamic quenching Fluorescence spectroscopy Human serum albumin Iohexol Molecular docking spectroscopic techniques liquid-chromatography mass-spectrometry modeling methods bovine fluorescence binding protein acid drug Chemistry Physics
Divisions:
Page Range: pp. 459-467
Journal or Publication Title: Journal of Molecular Liquids
Journal Index: ISI
Volume: 248
Identification Number: https://doi.org/10.1016/j.molliq.2017.10.096
ISSN: 0167-7322
Depositing User: مهندس مهدی شریفی
URI: http://eprints.bmsu.ac.ir/id/eprint/4112

Actions (login required)

View Item View Item