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• W2324854441 abstract "The crucial step for the fatal neurodegenerative prion diseases involves the conversion of a normal cellular protein, PrP(C), into a fibrous pathogenic form, PrP(Sc), which has an unusual stability against heat and resistance against proteinase K digestion. A successful challenge to reverse the reaction from PrP(Sc) into PrP(C) is considered valuable, as it would give a key to dissolving the complex molecular events into thermodynamic and kinetic analyses and may also provide a means to prevent the formation of PrP(Sc) from PrP(C) eventually in vivo. Here we show that, by applying pressures at kbar range, the proteinase K-resistant fibrils (rHaPrP(res)) prepared from hamster prion protein (rHaPrP [23-231]) by seeding with brain homogenate of scrapie-infected hamster, becomes easily digestible. The result is consistent with the notion that rHaPrP(res) fibrils are dissociated into rHaPrP monomers under pressure and that the formation of PrP(Sc) from PrP(C) is thermodynamically controlled. Moreover, the efficient degradation of prion fibrils under pressure provides a novel means of eliminating infectious PrP(Sc) from various systems of pathogenic concern." @default.
• W2324854441 created "2016-06-24" @default.
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• W2324854441 date "2014-07-04" @default.
• W2324854441 modified "2023-09-23" @default.
• W2324854441 title "Pressure-assisted dissociation and degradation of “proteinase K-resistant” fibrils prepared by seeding with scrapie-infected hamster prion protein" @default.
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• W2324854441 doi "https://doi.org/10.4161/pri.32081" @default.
• W2324854441 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4601478" @default.
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• W2324854441 hasPublicationYear "2014" @default.
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