albumin - publications

Predict more albumin - ligand interactions now!


1. Spectrochim Acta A Mol Biomol Spectrosc. 2011 Dec 29;89C:177-186. [Epub ahead of
print]

Comparative spectroscopic studies on drug binding characteristics and protein
surface hydrophobicity of native and modified forms of bovine serum albumin:
Possible relevance to change in protein structure/function upon non-enzymatic
glycation.

Khodarahmi R, Karimi SA, Ashrafi Kooshk MR, Ghadami SA, Ghobadi S, Amani M.

Medical Biology Research Center, Kermanshah University of Medical Sciences,
Kermanshah, Iran; Department of Pharmacognosy and Biotechnology, Faculty of
Pharmacy, P.O. Box 67145-1673, Kermanshah University of Medical Sciences,
Kermanshah, Iran.

The interaction between serum albumin (SA) and drugs has provided an interesting
ground for understanding of drug effects, especially in drug distribution and
drug-drug interaction on SA, in the case of multi-drug therapy. Determination of
the impact of various factors on drug-protein interaction is especially important
upon significant binding of drug to albumin. In the present study, the
interaction of two drugs (furosemide and indomethacin) with native and modified
albumins were investigated by using various spectroscopic methods. Fluorescence
data indicated that 1:1 binding of drugs to bovine serum albumin (BSA) is
associated with quenching of albumin intrinsic fluorescence. The Job's plot also
confirmed that drug binds to BSA via mentioned stoichiometry. Analysis of the
quenching and thermodynamic parameters indicated that intermolecular interactions
between drug and albumin may change upon protein modification. The theoretical
analyses also suggested some conformational changes of interacting side chains in
subdomain IIA binding site (at the vicinity of W(237)), which were in good
agreement with experimental data. Decrease of protein surface hydrophobicity
(PSH) was also observed upon both albumin modification and drug binding.

Copyright © 2011 Elsevier B.V. All rights reserved.

PMID: 22261105 [PubMed - as supplied by publisher]