Document Detail


The Rich Electrochemistry and Redox Reactions of the Copper Sites in the Cellular Prion Protein.
MedLine Citation:
PMID:  23144499     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
This paper reviews recent electrochemical studies of the copper complexes of prion protein (PrP) and its related peptides, and correlates their redox behavior to chemical and biologically relevant reactions. Particular emphasis is placed on the difference in redox properties between copper in the octarepeat (OR) and the non-OR domains of PrP, as well as differences between the high and low copper occupancy states in the OR domain. Several discrepancies in literature concerning these differences are discussed and reconciled. The PrP copper complexes, in comparison to copper complexes of other amyloidogenic proteins/peptides, display a more diverse and richer redox chemistry. The specific protocols and caveats that need to be considered in studying the electrochemistry and redox reactions of copper complexes of PrP, PrP-derived peptides, and other related amyloidogenic proteins are summarized.
Authors:
Feimeng Zhou; Glenn L Millhauser
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-5-4
Journal Detail:
Title:  Coordination chemistry reviews     Volume:  256     ISSN:  0010-8545     ISO Abbreviation:  Coord Chem Rev     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-11-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0271103     Medline TA:  Coord Chem Rev     Country:  -    
Other Details:
Languages:  ENG     Pagination:  2285-2296     Citation Subset:  -    
Affiliation:
Department of Chemistry and Biochemistry, California State University, Los Angeles, Los Angeles, California 90032.
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