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, PrPSc was not retained at all by such resin. This constitutes a new prion-specific property of PrPSc, which in addition to protease resistance and beta -sheet content, may result from its aberrant conformation.