Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases |
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| Authors: | Abdul‐Hamid M. Emwas Zeyad A. Al‐Talla Xianrong Guo Suliman Al‐Ghamdi Harbi T. Al‐Masri |
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| Affiliation: | 1. NMR Core Lab, King Abdullah University of Science and Technology, , Thuwal, Kingdom of Saudi Arabia;2. Analytical Core lab, King Abdullah University of Science and Technology, , Thuwal, Kingdom of Saudi Arabia;3. Princess Norah Oncology Center WR (King Abdullah Research Center), , Jeddah, Kingdom of Saudi Arabia;4. Faculty of Applied Sciences, Department of Applied Chemistry, Taibah University, , Madinah, 1343 Kingdom of Saudi Arabia |
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| 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. |
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| Keywords: | prion copper NMR EPR neurodegenerative disorder |
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