Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4923
Title: The dimeric and tetrameric octarepeat fragment of prion behaves differently to its monomeric unit
Authors: Valensin, Daniela 
M., Luczkowski
F., Mancini
A., Legowska
Gaggelli, Elena 
K., Rolka
Valensin, Gianni 
H., Kozlowski
Keywords: copper-binding; Cu(II) ions; coordination; complexes; domain
Issue Date: 2004
Project: None 
Journal: DALTON TRANSACTIONS
Abstract: 
Potentiometric and spectroscopic data have shown that octarepeat dimer and tetramer are much more effective ligands for Cu(II) ions than simple octapeptide. Thus, the whole N-terminal segment of prion protein due to cooperative effects, could be more effective in binding of Cu(II) than simple peptides containing a His residue. The gain of the Cu(II) binding by longer octarepeat peptides derives from the involvement of up to four imidazoles in the coordination of the first Cu(II) ion. This type of binding increases the order of the peptide structure, which allows successive metal ions for easier coordination.
Description: 
37226
URI: http://hdl.handle.net/20.500.12779/4923
ISSN: 1477-9226
DOI: 10.1039/b402090a
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