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Updated: Aug 18, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
[Prion protein and copper: a mysterious relationship]
W Rachidi1, J Riondel, H M McMahon
1Industrial Microbiology, University College Dublin (UCD), Belfield, Ireland. wrachidi@yahoo.com
Abstract:
Prion diseases form a group of fatal neurodegenerative disorders including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in animals. All of which are characterized by the accumulation of abnormally folded isoform of the cellular prion protein (PrP(C)), denoted PrP(Sc), which is the major component of infectious prion diseases. The function of PrP(C) remains elusive. Its amino-terminal region contains a repeated five octapeptide domain that binds copper. The protein is believed to display a superoxide dismutase like activity, and hence a possible protective function against oxidative stress. In this review, relationship between PrP, copper and oxidative stress was analysed. Thus, metal ions and oxidative stress would play an essential role in the pathogenesis of prion diseases and represent important targets for future therapeutic targets or a novel diagnostic marker.
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