✦ LIBER ✦

Structural changes of human serum albumin in response to a low concentration of heavy ions

✍ Scribed by Anushree Saha; Vladislav V. Yakovlev

Publisher: John Wiley and Sons
Year: 2010
Tongue: English
Weight: 476 KB
Volume: 3
Category: Article
ISSN: 1864-063X
DOI: 10.1002/jbio.201000044

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✦ Synopsis

Abstract

Lead ions in solution interact strongly with human serum albumin and modify the properties and function of albumin molecules. In the present study, we used optical spectroscopic techniques to explore the binding sites of lead, present in albumin. Structural and chemical analysis of albumin molecules using fluorescence and Raman spectroscopy, predicted the modification of two major amino acids in albumin due to lead binding. No secondary structural changes are observed in the protein molecule, which is further confirmed using circular dichroism absorption measurements. The results indicate that loss of charge from the binding site of albumin by the charged lead ions, give rise to dipole interaction which acts as the major contributor to promote protein agglomeration. (© 2010 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)

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