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Updated: Jun 29, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Binding of Ni2+ and Cu2+ ions to peptides with a Cys-His motif
Kinga Kulon1, Daniela Valensin, Wojciech Kamysz
1Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383, Wrocław, Poland.
Abstract:
Waglerin I is a 22 amino acid snake venom toxin. Its three fragments (GGKPDLRPCHP-NH2, PCHYIPRPKPR-NH2, PCHPPCHYIPR-NH2), due to the presence of two Cys and His residues, are potentially very attractive ligands for transition metal ions. The main aim of this work was to establish the impact of these two adjacent residues on Ni2+ ion binding, especially because this kind of motif is very common in nature, and the study of low molecular weight models could be helpful in understanding larger systems. In this work waglerin fragments and their N-protected analogues were studied with Ni2+ (and Cu2+ for peptides with disulfide bridges) ions using combined potentiometric and spectroscopic measurements (UV-Vis, CD, EPR and NMR). In all peptides, except PCHPPCHYIPR-NH2 with a disulfide bridge, the Cys-His motif was found to be crucial for the coordination of Ni2+ ions. In the case of the N-unprotected analogues, the N-terminal amino group participates in the coordination as well.
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