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Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: A spectroscopic study in combination with molecular docking and molecular dynamics simulation

Paper ID Volume ID Publish Year Pages File Format Full-Text
27266 44013 2012 9 PDF Available
Title
Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: A spectroscopic study in combination with molecular docking and molecular dynamics simulation
Abstract

Binding interaction of plasma protein bovine serum albumin (BSA) with external flexible charge transfer fluorophore 5-(4-dimethylamino-phenyl)-penta-2,4-dienenitrile (DMAPPDN) has been explored at physiological pH (7.4) by steady state absorption, emission, fluorescence anisotropy, Red Edge Excitation Shift (REES), far-UV circular dichroism (CD), time resolved spectral measurements in combination with molecular docking and molecular dynamics (MD) simulation studies. Chemical denaturation of the protein bound probe by guanidine hydrochloride (GdnHCl) has also been tracked using the spectral response of DMAPPDN. Interaction of the probe with BSA is reflected by the massive blue shift of the fluorophore emission maxima (78 nm) with the enhancement of fluorescence intensity due to change of hydrophobic micro-environment of the probe compared to a little change in protein secondary structure. Benesi–Hildebrand plot reveals spontaneous formation of 1:1 BSA–DMAPPDN complex with binding constant 8.821 ± 0.01 × 103 M−1 and binding free energy change −5.359 kcal mol−1. Molecular docking study supports the binding of probe in the hydrophobic cavity of sub domain IIA of BSA. The distance for energy transfer from tryptophan of BSA to DMAPPDN measured from fluorescence resonance energy transfer (FRET) results is in good agreement with results of molecular docking study. MD simulation predicts greater stability of BSA–DMAPPDN complex compared to the free protein.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Interaction of small fluorophore with plasma protein BSA studied spectroscopically. ► FRET from tryptophan of BSA to probe. ► molecular docking and molecular dynamics simulation complement experimental results. ► Tracking of chemical denaturation of protein by this extrinsic fluorescence probe.

Keywords
BSA; Molecular docking; MD simulation; 5-(4-Dimethylamino-phenyl)-penta-2,4-dienenitrile; FRET
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Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: A spectroscopic study in combination with molecular docking and molecular dynamics simulation
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 231, Issue 1, 1 March 2012, Pages 19–27
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