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Updated: Jun 20, 2026
Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Evaluation of copper2+ affinities for the prion protein
Rebecca C Nadal1, Paul Davies, David R Brown
1School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.
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The prion protein (PrP) is a cell-surface Cu2+ binding glycoprotein which can 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.
