Copper Binding to the PrP Isoforms: a Putative Marker of Their Conformation and Function

We show here that PrPC, the normal isoform of the prion protein (PrPSc), could be retained by a Cu2+-loaded resin through two different binding sites. Contrarily, PrPScwas not retained at all by such resin. This constitutes a new prion-specific property of PrPSc, which in addition to protease resistance and β-sheet content, may result from its aberrant conformation.