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Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
Author(s) -
Emwas AbdulHamid M.,
AlTalla Zeyad A.,
Guo Xianrong,
AlGhamdi Suliman,
AlMasri Harbi T.
Publication year - 2013
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.3936
Subject(s) - chemistry , gene isoform , copper , prion protein , electron paramagnetic resonance , nuclear magnetic resonance spectroscopy , glycoprotein , conformational change , biophysics , mechanism (biology) , biochemistry , neuroscience , disease , nuclear magnetic resonance , stereochemistry , pathology , biology , medicine , gene , physics , philosophy , organic chemistry , epistemology
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.