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

Handle URI:
http://hdl.handle.net/10754/566051
Title:
Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
Authors:
Emwas, Abdul-Hamid M.; Al-Talla, Zeyad; Guo, Xianrong; Al-Ghamdi, Suliman; Al-Masri, Harbi Tomah
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.
KAUST Department:
Advanced Nanofabrication, Imaging and Characterization Core Lab; Analytical Core Lab
Publisher:
Wiley-Blackwell
Journal:
Magnetic Resonance in Chemistry
Issue Date:
24-Feb-2013
DOI:
10.1002/mrc.3936
PubMed ID:
23436479
Type:
Article
ISSN:
07491581
Sponsors:
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.
Appears in Collections:
Articles; Analytical Core Lab; Advanced Nanofabrication, Imaging and Characterization Core Lab

Full metadata record

DC FieldValue Language
dc.contributor.authorEmwas, Abdul-Hamid M.en
dc.contributor.authorAl-Talla, Zeyaden
dc.contributor.authorGuo, Xianrongen
dc.contributor.authorAl-Ghamdi, Sulimanen
dc.contributor.authorAl-Masri, Harbi Tomahen
dc.date.accessioned2015-08-12T09:01:07Zen
dc.date.available2015-08-12T09:01:07Zen
dc.date.issued2013-02-24en
dc.identifier.issn07491581en
dc.identifier.pmid23436479en
dc.identifier.doi10.1002/mrc.3936en
dc.identifier.urihttp://hdl.handle.net/10754/566051en
dc.description.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.en
dc.description.sponsorshipWe 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.en
dc.publisherWiley-Blackwellen
dc.subjectcopperen
dc.subjectEPRen
dc.subjectneurodegenerative disorderen
dc.subjectNMRen
dc.subjectprionen
dc.titleUtilizing NMR and EPR spectroscopy to probe the role of copper in prion diseasesen
dc.typeArticleen
dc.contributor.departmentAdvanced Nanofabrication, Imaging and Characterization Core Laben
dc.contributor.departmentAnalytical Core Laben
dc.identifier.journalMagnetic Resonance in Chemistryen
dc.contributor.institutionFaculty of Applied Sciences, Department of Applied Chemistry, Taibah University, Madinah 1343, Saudi Arabiaen
kaust.authorEmwas, Abdul-Hamid M.en
kaust.authorAl-Talla, Zeyaden
kaust.authorGuo, Xianrongen

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