Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
Type
ArticleKAUST Department
Advanced Nanofabrication, Imaging and Characterization Core LabAnalytical Chemistry Core Lab
Analytical Core Lab
Imaging and Characterization Core Lab
Date
2013-02-24Online Publication Date
2013-02-24Print Publication Date
2013-05Permanent link to this record
http://hdl.handle.net/10754/566051
Metadata
Show full item recordAbstract
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 (PrPC) and a disease-associated isoform (PrPSc). Prion diseases are a group of lethal neurodegenerative disorders that develop as a result of conformational conversion of PrPC into PrPSc. 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.Citation
Emwas, A.-H. M., Al-Talla, Z. A., Guo, X., Al-Ghamdi, S., & Al-Masri, H. T. (2013). Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Magnetic Resonance in Chemistry, 51(5), 255–268. doi:10.1002/mrc.3936Sponsors
We thank King Abdullah University of Science and Technology (KAUST) for the financial support. Special thanks to Dr. Jamil Saad from the University of Alabama at Birmingham, USA, and Dr. Virginia Unkefer from KAUST for their assistance and helpful remarks.Publisher
WileyJournal
Magnetic Resonance in ChemistryDOI
10.1002/mrc.3936PubMed ID
23436479ae974a485f413a2113503eed53cd6c53
10.1002/mrc.3936
Scopus Count
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