Prion diseases are characterized by the conversion of normal prion protein (PrP) into its infectious isoform PrPSc. Human PrP is known to bind Cu in the N-terminal region, and the region around histidine residues 96 and 111 has been proposed to be key for the conversion of PrP to PrPSc. Cu(II) binding to these sites has been extensively studied by spectroscopic and theoretical tools, using model peptide fragments containing His96 and/or His111. A summary of the copper coordination properties of His96 and His111 in these fragments will be presented, discussing their electronic structure and the Cotton effect of their d-d transitions. In order to understand the redox properties of these copper-peptide complexes, a study of their reduction by ascorbate and re-oxidation by molecular oxygen is underway. These results will be presented, along with electronic structure calculations that help evaluate different coordination models for the reduced form of these complexes.

Copper binding to human prion protein fragments: Coordination and redox properties

243rd National Meeting (2012)

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