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Wiley, Angewandte Chemie International Edition, 36(47), p. 6888-6891, 2008

DOI: 10.1002/anie.200800677

Wiley, Angewandte Chemie, 36(120), p. 6994-6997, 2008

DOI: 10.1002/ange.200800677

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Cyclic peptides bearing a side-chain tail: A tool to model the structure and reactivity of protein zinc sites.

Journal article published in 2008 by Olivier Sénèque Dr, Olivier Sénèque, Emilie Bourlès, Emilie Bourlès Dr, Vincent Lebrun, Estelle Bonnet, Pascal Dumy Prof. Dr, Pascal Dumy ORCID, Jean-Marc Latour Dr, Jean-Marc Latour
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Abstract

A new peptide design has been introduced to model the tetracysteinate zinc sites involving CXXC motifs present in beta-hairpins. It is based on a cyclic peptide incorporating one CXXC motif in addition to a variable CXC motif in a linear chain grafted onto the cycle via a glutamate or a lysine side chain. This 20-amino acid design has been used to model the Zn(Cys)4 sites of the heat shock protein Hsp33. TheZn2+ and Co2+ complexes were characterized by UV/vis, CD and NMR spectroscopy. The structures of two metallated peptides were solved by NMR. An excellent similarly was achieved between the model peptide and the target protein, both at the metal binding site and in the surrounding hydrogen bond network. Preliminary reactivity studies toward H2O2 are reported and show that the best model fit the kinetics observed for Hsp33.