Fibrillization of Recombinant Bovine Prion Protein (rec-PrP) In vitro

摘要

Conversion of normal prion protein (PrP~c) from the conformation with predominantly α-helical structure into the conformation rich in p-structures (PrP~(sc), P-PrP, and PrP~(res)) underlies the pathogenesis of prion diseases, a special class of degenerative diseases of the nervous system of humans and animals. Prion diseases, or transmissible spongiform encephalopathies (TSEs) of humans, include the Creutzfeldt-Jakob disease (CJD), the Gerstmann-Straussler-Scheinker syndrome, new variant of CJD, kuru, as well as the fatal familial insomnia. The most well-known transmissible spongiform encephalopathies of animals are scrapie of sheep, chronic wasting disease of deer and moose, and bovine spongiform encephalopathy (mad cow disease) [1].