NMR paper Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.

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[NMR paper] Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.

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02-26-2013, 06:35 PM

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Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.

Magn Reson Chem. 2013 Feb 24;

Authors: Emwas AH, Al-Talla ZA, Guo X, Al-Ghamdi S, Al-Masri HT

Abstract
Copper is an essential nutrient for the normal development of the brain and nervous system, although the hallmark of several neurological diseases is a change in copper concentrations in the brain and central nervous system. Prion protein (PrP) is a copper-binding, cell-surface glycoprotein that exists in two alternatively folded conformations: a normal isoform (PrP(C) ) and a disease-associated isoform (PrP(Sc) ). Prion diseases are a group of lethal neurodegenerative disorders that develop as a result of conformational conversion of PrP(C) into PrP(Sc) . The pathogenic mechanism that triggers this conformational transformation with the subsequent development of prion diseases remains unclear. It has, however, been shown repeatedly that copper plays a significant functional role in the conformational conversion of prion proteins. In this review, we focus on current research that seeks to clarify the conformational changes associated with prion diseases and the role of copper in this mechanism, with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins. Copyright © 2013 John Wiley & Sons, Ltd.

PMID: 23436479 [PubMed - as supplied by publisher]

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