Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
KAUST DepartmentImaging and Characterization Core Lab
Analytical Core Lab
Advanced Nanofabrication, Imaging and Characterization Core Lab
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AbstractCopper 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.
SponsorsWe 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.
JournalMagnetic Resonance in Chemistry
- Conformational conversion of prion protein in prion diseases.
- Authors: Zhou Z, Xiao G
- Issue date: 2013 Jun
- Prion disease: A loss of antioxidant function?
- Authors: Wong BS, Pan T, Liu T, Li R, Petersen RB, Jones IM, Gambetti P, Brown DR, Sy MS
- Issue date: 2000 Aug 28
- Comparative analysis of the human and chicken prion protein copper binding regions at pH 6.5.
- Authors: Redecke L, Meyer-Klaucke W, Koker M, Clos J, Georgieva D, Genov N, Echner H, Kalbacher H, Perbandt M, Bredehorst R, Voelter W, Betzel C
- Issue date: 2005 Apr 8
- Evolving views in prion glycosylation: functional and pathological implications.
- Authors: Ermonval M, Mouillet-Richard S, Codogno P, Kellermann O, Botti J
- Issue date: 2003 Jan-Feb
- Prion proteins leading to neurodegeneration.
- Authors: La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
- Issue date: 2008 Dec