albumin - publications

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1. Environ Toxicol Pharmacol. 2011 Dec 31;33(2):327-333. [Epub ahead of print]

The influence of Cd(2+), Hg(2+) and Pb(2+) on taxifolin binding to bovine serum
albumin by spectroscopic methods: With the viewpoint of toxic ions/drug
interference.

Peng M, Shi S, Zhang Y.

Key Laboratory of Hunan Forest Products and Chemical Industry Engineering, Jishou
University, Zhangjiajie 427000, China; School of Chemistry and Chemical
Engineering, Central South University, Changsha 410083, China.

The effect of heavy metal ions, Cd(2+), Hg(2+) and Pb(2+) on taxifolin binding to
bovine serum albumin (BSA) has been investigated by spectroscopic methods. The
results indicated that the presence of heavy metal ions significantly affected
the binding modes and binding affinities of taxifolin to BSA, and the effects
depended on the type of heavy metal ions. One binding mode was found for
taxifolin with and without Cd(2+), while two binding modes-a weaker one at low
concentration and a stronger one at high concentration-were found for taxifolin
in the presence of Hg(2+) and Pb(2+). Cd(2+) decreased the binding affinity of
taxifolin for BSA by 7.3%; however, Hg(2+) increased the binding affinity of
taxifolin for BSA by 13.3% in lower concentration and 33.3% in higher
concentration. Pb(2+) decreased the binding affinity of taxifolin for BSA by
28.4% in lower concentration, and increased the binding affinity of taxifolin for
BSA by 20.6% in higher concentration. The decreased binding affinity of taxifolin
for BSA in the presence of Cd(2+) was mainly because of the existence of
competitive binding between taxifolin and Cd(2+). However, the conformational
change of BSA may the main reason for the changed binding affinity and binding
distance of taxifolin for BSA in the presence of Hg(2+) and Pb(2+).

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

PMID: 22301163 [PubMed - as supplied by publisher]