Protocol

Prion Protein Protocols

Volume 459 of the series Methods in Molecular Biology™ pp 105-115

Methods for Conversion of Prion Protein into Amyloid Fibrils

  • Leonid BreydoAffiliated withMedical Biotechnology Center, University of Maryland Biotechnology Institute
  • , Natallia MakaravaAffiliated withMedical Biotechnology Center, University of Maryland Biotechnology Institute
  • , Ilia V. BaskakovAffiliated withMedical Biotechnology Center, University of Maryland Biotechnology Institute

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Summary

Misfolding and aggregation of prion protein (PrP) is related to several neurodegenerative diseases in humans such as Creutzfeldt—Jacob disease, fatal familial insomnia, and Gerstmann—Straussler—Sheinker disease. Amyloid fibrils prepared from recombinant PrP in vitro share many features of the infectious prions. These fibrils can be used as a synthetic surrogate of PrPSc for development of prion diagnostics, including generation of PrPSc-specific antibody, for screening of antiprion drugs, or for development of antiprion decontamination procedures. Here, we describe the methods of preparation of prion protein fibrils in vitro and biochemical assays for assessing physical properties and the quality of fibrils.

Keywords

Amyloid fibrils conformational transition prion diseases recombinant prion protein