Copper binding to the PrP isoforms: a putative marker of their conformation and function

We show here that PrP(C), the normal isoform of the prion protein (PrP(Sc)), could be retained by a Cu(2+)-loaded resin through two different binding sites. Contrarily, PrP(Sc) was not retained at all by such resin. This constitutes a new prion-specific property of PrP(Sc), which in addition to protease resistance and beta-sheet content, may result from its aberrant conformation.