Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
Article first published online: 24 FEB 2013
Copyright © 2013 John Wiley & Sons, Ltd.
Magnetic Resonance in Chemistry
Volume 51, Issue 5, pages 255–268, May 2013
How to Cite
Emwas, A.-H. M., Al-Talla, Z. A., Guo, X., Al-Ghamdi, S. and Al-Masri, H. T. (2013), Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Magn. Reson. Chem., 51: 255–268. doi: 10.1002/mrc.3936
- Issue published online: 14 APR 2013
- Article first published online: 24 FEB 2013
- Manuscript Accepted: 11 JAN 2013
- Manuscript Revised: 19 DEC 2012
- Manuscript Received: 30 APR 2012
- neurodegenerative disorder
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.