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Probing HSA-ionic liquid interactions by spectroscopic and molecular docking methods

Paper ID Volume ID Publish Year Pages File Format Full-Text
30279 44468 2014 9 PDF Available
Title
Probing HSA-ionic liquid interactions by spectroscopic and molecular docking methods
Abstract

•BMOP quenches the fluorescence intensity of HSA and changes its conformation.•Quenching follows the mixed quenching mechanism.•The hydrophobic force played a key role in the interaction process.•For the first time, we report on the interaction between pyrrolidinium based ionic liquid (BMOP) and HSA.

Herein, we report the interaction of synthesized pyrrolidinium based ionic liquid, N-butyl-N-methyl-2-oxopyrrolidinium bromide (BMOP) with human serum albumin (HSA). The BMOP was characterized by using 1H NMR, 13C NMR and FT-IR techniques. The critical micelle concentration (cmc) of BMOP was confirmed by surface tension, conductivity and contact angle measurements. The interactions between HSA and BMOP were studied by steady-state and time-resolved fluorescence, UV–visible, FT-IR spectroscopic and molecular docking methods. The steady-state fluorescence spectra showed that BMOP quenched the fluorescence of HSA through combined quenching mechanism. Corresponding thermodynamic parameters viz. Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) illustrated that the binding process was spontaneous and entropy driven. It is also suggested that hydrophobic forces play a key role in the binding of BMOP to HSA. In addition, the pyrene probe analysis again suggests the involvement of hydrophobic interaction in HSA–BMOP complex formation. Surface tension profile showed that the cmc value of BMOP in the presence of HSA is higher than the cmc value of pure BMOP. The FT-IR results show a conformational change in the secondary structure of HSA upon the addition of BMOP. The molecular docking result indicated that BMOP binds with HSA at hydrophobic pocket domain IIA with hydrophobic and hydrogen bond interactions in which hydrophobic interactions are dominating.

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Keywords
Ionic liquid; Human serum albumin; Quenching; Hydrophobic interactions; Molecular docking
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Probing HSA-ionic liquid interactions by spectroscopic and molecular docking methods
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 138, 5 September 2014, Pages 27–35
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us