Cysteine based ferrocenyl peptides as heavy metal sensors

BIOL 205

Conor Scully, conor.scully@ucd.ie, Centre for Synthesis and Chemical Biology, School of Chemistry, University College Dublin, Belfield, Dublin 4, Ireland and Peter J. Rutledge, p.rutledge@chem.usyd.edu.au, School of Chemistry, University of Sydney, Sydney, NSW 2006, Australia.
The aim of this project is to synthesise cadmium- and mercury-specific molecules based on metallothioneins, cysteine-rich mammalian proteins which perform heavy metal binding functions in vivo. The template for these molecules are short-chain peptides in which at least half of the amino acid residues are cysteine, the remainder being residues with non-polar side chains such as phenylalanine, valine and glycine to probe metric and steric effects. The target molecules also incorporate sensor functionality through attachment to ferrocene. This is advantageous due to the high stability of ferrocenyl peptides in solution and to the presence of the Fe(II)/Fe(III) redox couple which provides a convenient electrochemical probe to study binding events between the peptides and heavy metal ions in solution
 

Enzymes
4:30 PM-6:30 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster

Division of Biological Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006