title: Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.
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 (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.
authors: NMR Core Lab, King Abdullah University of Science and Technology, Thuwal, Kingdom of Saudi Arabia. abdelhamid.emwas@kaust.edu.sa
authors: Abdul-Hamid M
authors: AH
authors: Emwas
authors: Zeyad A
authors: ZA
authors: Al-Talla
authors: Xianrong
authors: X
authors: Guo
authors: Suliman
authors: S
authors: Al-Ghamdi
authors: Harbi T
authors: HT
authors: Al-Masri
mesh_terms: D000818:Animals; D003300:Copper / Q000032:analysis* / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D017096:Prion Diseases / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism
chemical_list: D011328:Prions; D003300:Copper