Methods for Conversion of Prion Protein into Amyloid Fibrils

  • Leonid Breydo
  • Natallia Makarava
  • Ilia V. Baskakov
Part of the Methods in Molecular Biology™ book series (MIMB, volume 459)


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.


Amyloid fibrils conformational transition prion diseases recombinant prion protein 


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Copyright information

© Humana Press, a part of Springer Science + Business Media, LLC 2008

Authors and Affiliations

  • Leonid Breydo
    • 1
  • Natallia Makarava
    • 1
  • Ilia V. Baskakov
    • 1
  1. 1.Medical Biotechnology CenterUniversity of Maryland Biotechnology InstituteBaltimoreUSA

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