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Interaction of thimerosal with proteins—ethylmercury adduct formation of human serum albumin and β-lactoglobulin A

Stefan Trümpler,a  Wiebke Lohmann,a  Björn Meermann,a  Wolfgang Buscher,a  Michael Sperlingab  and  Uwe Karst*a 
Author affiliations

* Corresponding authors

a University of Münster, Institute of Inorganic and Analytical Chemistry, Corrensstr. 30, Münster, Germany
E-mail: uk@uni-muenster.de
Fax: +49 251 83 36013
Tel: +49 251 83 33141

b European Virtual Institute for Speciation Analysis, Mendelstr. 11, Münster, Germany

Abstract

The interaction of thimerosal, an ethylmercury-containing bactericide and fungicide used as preservative in vaccines and other drugs, with free thiols in proteins has been investigated using gradient reversed phase liquid chromatography (LC) with inductively coupled plasma mass spectrometry (ICP-MS) and electrospray mass spectrometry (ESI-MS) detection. As model proteins, β-lactoglobulin A (18.4 kDa) from bovine milk and human serum albumin (66.5 kDa) have been used. Physiological conditions upon an intravenous injection of thimerosal-containing drugs were mimicked. The formation of ethylmercury–protein adducts was proved and the identification of the binding site of ethylmercury, a free thiol residue in the peptide T13 was achieved after tryptic digestion of β-lactoglobulin A.

Graphical abstract: Interaction of thimerosal with proteins—ethylmercury adduct formation of human serum albumin and β-lactoglobulin A

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Publication details

The article was received on 12 Sep 2008, accepted on 15 Oct 2008 and first published on 01 Jan 2008


Article type: Paper
DOI: 10.1039/B815978E
Citation: Metallomics, 2009,1, 87-91

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    Interaction of thimerosal with proteins—ethylmercury adduct formation of human serum albumin and β-lactoglobulin A

    S. Trümpler, W. Lohmann, B. Meermann, W. Buscher, M. Sperling and U. Karst, Metallomics, 2009, 1, 87
    DOI: 10.1039/B815978E

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