albumin - publications

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1. Ecotoxicol Environ Saf. 2012 Jan 30. [Epub ahead of print]

Human serum albumin stability and toxicity of anthraquinone dye alizarin
complexone: An albumin-dye model.

Ding F, Zhang L, Diao JX, Li XN, Ma L, Sun Y.

Department of Chemistry, China Agricultural University, Beijing 100193, China;
Department of Biological Engineering, Massachusetts Institute of Technology,
Cambridge, MA 02139, USA.

The complexation between the primary vector of ligands in blood plasma, human
serum albumin (HSA) and a toxic anthraquinone dye alizarin complexone, was
unmasked by means of circular dichroism (CD), molecular modeling, steady state
and time-resolved fluorescence, and UV/vis absorption measurements. The
structural investigation of the complexed HSA through far-UV CD,
three-dimensional and synchronous fluorescence shown the polypeptide chain of HSA
partially destabilizing with a reduction of α-helix upon conjugation. From
molecular modeling and competitive ligand binding results, Sudlow's site I, which
was the same as that of warfarin-azapropazone site, was appointed to retain
high-affinity for alizarin complexone. Moreover, steady state fluorescence
displayed that static type and Förster energy transfer is the operational
mechanism for the vanish in the tryptophan (Trp)-214 fluorescence, this
corroborates time-resolved fluorescence that HSA-alizarin complexone adduct
formation has an affinity of 10(5)M(-1), and the driving forces were found to be
chiefly π-π, hydrophobic, and hydrogen bonds, associated with an exothermic free
energy change. These data should be utilized to illustrate the mechanism by which
the toxicological action of anthraquinone dyes is mitigated by transporter HSA.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID: 22296882 [PubMed - as supplied by publisher]