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. Certain applications in prion area require recombinant PrP of high purity and quality. Here, we report an experimental procedure for expression and purification of full-length mammalian PrP. This protocol has been proved to yield PrP of extremely high purity that lacks PrP adducts, which are normally generated as a result of spontaneous oxidation or degradation. We also describe methods for the preparation of amyloid fibrils from recombinant PrP in vitro. Recombinant PrP fibrils can be used as a noninfectious synthetic surrogate of PrPSc for development of prion diagnostics including the generation of PrP Sc-specific antibody. © 2012 Springer Science+Business Media, LLC.
CITATION STYLE
Makarava, N., & Baskakov, I. V. (2012). Purification and fibrillation of full-length recombinant PrP. Methods in Molecular Biology, 849, 33–52. https://doi.org/10.1007/978-1-61779-551-0_4
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