Evaluation of Copper(2+) Affinities for the Prion Protein

R C Nadal, P Davies, D R Brown, J H Viles

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

The prion protein (PrP) is a cell-surface Cu2+ binding glcoprotein which call bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.
Original languageEnglish
Pages (from-to)8929-8931
Number of pages3
JournalBiochemistry
Volume48
Issue number38
DOIs
Publication statusPublished - Aug 2009

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