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Study of microheterogeneous environment of protein Human Serum Albumin by an extrinsic fluorescent reporter: A spectroscopic study in combination with Molecular Docking and Molecular Dynamics Simulation

Paper ID Volume ID Publish Year Pages File Format Full-Text
30814 44505 2012 11 PDF Available
Title
Study of microheterogeneous environment of protein Human Serum Albumin by an extrinsic fluorescent reporter: A spectroscopic study in combination with Molecular Docking and Molecular Dynamics Simulation
Abstract

We report extrinsic fluorescent probe 5-(4-dimethylamino-phenyl)-penta-2,4-dienoic acid (DMAPPDA) as a molecular reporter for studying microheterogeneous environment of protein Human Serum Albumin (HSA) via spectral modification of the probe under physiological condition. Steady state emission, fluorescence anisotropy, Red Edge Excitation Shift (REES), far-UV Circular Dichroism (CD), Atomic Force Microscopy (AFM) imaging, time resolved spectral measurements, Molecular Docking and Molecular Dynamics (MD) Simulation techniques have been used to fulfill this achievement. Interaction of the probe with HSA is signaled by the blue shift of the fluorophore emission maxima with enhancement of fluorescence intensity. The increase in steady state anisotropy, REES and fluorescence lifetime values with increasing protein concentrations indicates interaction and movement of the probe from free aqueous media to the more restricted less polar hydrophobic interior of protein. Experimental results obtained from Benesi–Hildebrand plot support the formation of 1:1 HSA–DMAPPDA complex with high binding constant and negative free energy change. Thermal denaturation of the probe bound protein has also been tracked using the spectral response of DMAPPDA. Molecular Docking studies revealed binding of the probe with in the hydrophobic cavity of subdomain IIA of HSA. MD Simulation supports greater stability of HSA–DMAPPDA complex compared to free protein.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Binding interaction of small extrinsic fluorophore with plasma protein HSA. ► Probe binding at hydrophobic cavity of subdomain IIA of HSA. ► Molecular Docking and Molecular Dynamics Simulation complement experimental results. ► Tracking of denaturation of protein by this extrinsic fluorescence probe.

Keywords
Extrinsic fluorescent probe; Human Serum Albumin; Fluorescence; Molecular Docking; Molecular Dynamics Simulation
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Study of microheterogeneous environment of protein Human Serum Albumin by an extrinsic fluorescent reporter: 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 B: Biology - Volume 112, 2 July 2012, Pages 48–58
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