albumin - publications

Predict more albumin - ligand interactions now!

1. J Photochem Photobiol B. 2012 Apr 19. [Epub ahead of print]

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.

Jana S, Dalapati S, Ghosh S, Guchhait N.

Department of Chemistry, University of Calcutta, 92 A.P.C. Road, Kolkata 700 009,

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.

Copyright © 2012 Elsevier B.V. All rights reserved.

PMID: 22575346 [PubMed - as supplied by publisher]