albumin - publications

Predict more albumin - ligand interactions now!


1. Talanta. 2012 Apr 15;92:45-52. Epub 2012 Jan 25.

The solvatochromic effects of side chain substitution on the binding interaction
of novel tricarbocyanine dyes with human serum albumin.

Beckford G, Owens E, Henary M, Patonay G.

Department of Chemistry, University Plaza, Georgia State University, Atlanta, GA
30303, USA.

The effects of solvatochromism on protein-ligand interactions have been studied
by absorbance and near-infrared laser induced fluorescence (NIR-LIF)
spectroscopy. The utility of three novel classes of cyanine dyes designed for
this purpose illustrates that the affinity interactions of ligands at the
hydrophobic binding pockets of Human Serum Albumin (HSA) are not only dependent
on the overall hydrophobic characteristics of the molecules but are highly
influenced by the size of the ligands as well. Whereas changes to the chromophore
moiety exhibited slight to moderate changes to the hydrophobic nature of these
molecules, substitution at the alkyl indolium side chain has enabled us to vary
the binding affinity towards serum albumin. Substitution at the indolium side
chain among an ethyl to butyl group results in improved binding characteristics
and an almost three-fold increase in affinity constant. In addition, replacement
of the ethyl side chain with a phenylpropyl group also yielded unique
solvotachromic patterns such as increased hydrophobicity and subsequent
biocompatibility with the HSA binding regions. Ligand interaction was however
inhibited by steric hindrance associated with the bulky phenyl ring system thus
affecting the increased binding that could be realized from the improved
hydrophobic nature of the molecules. This characteristic change in binding
affinity is of potential interest to developing a methodology which reveals
information on the hydrophobic character and steric specificity of the binding
cavities.

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

PMID: 22385806 [PubMed - in process]