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• W2015178568 abstract "The cellular prion protein (PrPC) binds to Cu2+ ions in vivo, and a misfolded form of PrPC is responsible for a range of transmissible spongiform encephalopathies. Recently, disruption of Cu2+ homeostasis in mice has been shown to impart resistance to scrapie infection. Using full-length PrPC and model peptide fragments, we monitor the sequential loading of Cu2+ ions onto PrPC using visible circular dichroism. We show the N-terminal amino group of PrPC is not the principal binding site for Cu2+; however, surprisingly, it has an affinity for Cu2+ tighter than that of the individual octarepeat binding sites present within PrPC. We re-evaluate what is understood about the sequential loading of Cu2+ onto the full-length protein and show for the first time that Cu2+ loads onto the N-terminal amino group before the single octarepeat binding sites." @default.
• W2015178568 created "2016-06-24" @default.
• W2015178568 creator A5007039104 @default.
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• W2015178568 date "2014-06-11" @default.
• W2015178568 modified "2023-09-24" @default.
• W2015178568 title "Copper(II) Sequentially Loads onto the N-Terminal Amino Group of the Cellular Prion Protein before the Individual Octarepeats" @default.
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• W2015178568 doi "https://doi.org/10.1021/bi500643b" @default.
• W2015178568 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24878028" @default.
• W2015178568 hasPublicationYear "2014" @default.
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