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

Abdul-Hamid M. Emwas, Zeyad Al-Talla, Xianrong Guo, Suliman Al-Ghamdi, Harbi Tomah Al-Masri

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

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 (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.
Original languageEnglish (US)
Pages (from-to)255-268
Number of pages14
JournalMagnetic Resonance in Chemistry
Volume51
Issue number5
DOIs
StatePublished - Feb 24 2013

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: 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.

ASJC Scopus subject areas

  • General Materials Science
  • General Chemistry

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