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Updated: Jul 17, 2025

A Study of the Complexation of MercuryII with Dicysteinyl Tetrapeptides by Electrospray Ionization Mass Spectrometry
Published on: January 8, 2016
Disclosing the Preferential Mercury Chelation by SeCys Containing Peptides over Their Cys Analogues
Mikel Bernabeu de Maria1, Diego Tesauro2, Filippo Prencipe3
1Pays de l'Adour, E2S UPPA, CNRS, IPREM, 64000 Pau, France.
Abstract:
Methylmercury, mercury (II), and mercury (I) chlorides were found to react with vasopressin, a nonapeptide hormone cyclized by two cysteine residues, and its mono- and diselenium analogues to form several mercury-peptide adducts. The replacement of Cys by SeCys in vasopressin increased the reactivity toward methylmercury, with the predominant formation of -Se/S-Hg-Se-bridged structures and the consequent demethylation of methylmercury. In competitive experiments, CH3HgCl reacted preferentially with the diselenium analogue rather than with vasopressin. The diselenium peptide also showed the capability to displace the CH3Hg moiety bound to S in vasopressin. These results open a promising perspective for the use of selenopeptides for methylmercury chelation and detoxification strategies.
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