Please use this identifier to cite or link to this item:
Title: Binding of Ni2+ and Cu2+ ions to peptides with a Cys-His motif
Authors: K., Kulon
Valensin, Daniela 
W., Kamysz
R., Nadolny
Gaggelli, Elena 
Valensin, Gianni 
H., Kozlowski
Issue Date: 2008
Project: None 
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.
ISSN: 1477-9226
DOI: 10.1039/B806851H
Appears in Collections:Publications

Show full item record

Page view(s)

Last Week
Last month
checked on May 8, 2021

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.