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Assembly of Natural and Recombinant Prion Protein Into Fibrils by Karl-Werner Leffers; Holger Wille; Jan Stöhr; Erika Junger; Stanley B. Prusiner; Detlev Riesner is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The conversion of the α-helical, cellular isoform of the prion protein (PrP^C^) to the insoluble, β-sheet-rich, infectious, disease-causing isoform (PrP^Sc^) is the fundamental event in the prion diseases. The C-terminal fragment of PrP^Sc^(PrP 27–30) is formed by limited proteolysis and retains infectivity. Unlike full-length PrP^Sc^, PrP 27–30 polymerizes into rod-shaped structures with the ultra-structural and tinctorial properties of amyloid. To study the folding of PrP, both with respect to the formation of PrP^Sc^from PrP^C^and the assembly of rods from PrP 27–30, we solubilized Syrian hamster (sol SHa) PrP 27–30 in low concentrations (0.2%) of sodium dodecyl sulfate (SDS) under conditions previously used to study the structural transitions of this protein. Sol SHaPrP 27–30 adopted a β-sheet-rich structure at SDS concentrations between 0.02% and 0.04% and remained soluble. Here we report that NaCl stabilizes SHaPrP 27–30 in a soluble, β-sheet-rich state that allows fibril assembly to proceed over several weeks. Under these conditions, fibril formation occurred not only with sol PrP 27–30, but also with native SHaPrP^C^. Addition of sphingolipids seems to increase

Who reads Assembly of Natural and Recombinant Prion Protein Into Fibrils?

Author

Karl-Werner Leffers; Holger Wille; Jan Stöhr; Erika Junger; Stanley B. Prusiner; Detlev Riesner

Publisher

Walter de Gruyter GmbH & Co. KG; Walter de Gruyter GmbH (ISSN 1431-6730)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)