Copper Binding to the PrP Isoforms: a Putative Marker of Their Conformation and Function
- 1 September 2001
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 75 (17), 7872-7874
- https://doi.org/10.1128/jvi.75.17.7872-7874.2001
Abstract
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.Keywords
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