The same primary structure of the prion protein yields two distinct self-propagating states.

ABSTRACT: The question of whether distinct self-propagating structures could be formed within the same amino acid sequence in the absence of external cofactors or templates has important implications for a number of issues, including the origin of prion strains and the engineering of smart, self-assembling peptide-based biomaterials. In the current study, we showed that chemically identical prion protein can give rise to conformationally distinct, self-propagating amyloid structures in the absence of cellular cofactors, post-translational modification, or PrP(Sc)-specified templates. Even more surprising, two self-replicating states were produced under identical solvent conditions, but under different shaking modes. Individual prion conformations were inherited by daughter fibrils in seeding experim

SUBMITTER: Makarava N 

PROVIDER: S-EPMC2414308 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature