2. Academic Validation
  3. Interaction of a ferrocenoyl-modified peptide with papain: toward protein-sensitive electrochemical probes

Interaction of a ferrocenoyl-modified peptide with papain: toward protein-sensitive electrochemical probes

  • Bioconjug Chem. 2003 May-Jun;14(3):601-6. doi: 10.1021/bc0256446.
Kevin Plumb 1,  Heinz-Bernhard Kraatz
Affiliations

Affiliation

  • 1 Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, SK S7N 5C9, Canada.
PMID: 12757385 DOI: 10.1021/bc0256446
Abstract

A new ferrocenoyl tetrapeptide, Fc-Gly-Gly-Tyr-Arg-OH, has been synthesized, which acts as an effective competitive inhibitor to papain, with a K(i) of 9 microM at pH 6.2. The electrochemical potential of the ferrocenoyl moiety is influenced by papain binding, resulting in a small cathodic shift of 30 mV.

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