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Title (Primary) Interactions of recombinant prions with compounds of therapeutical significance
Author Georgieva, D.; Schwark, D.; von Bergen, M.; Redecke, L.; Genov, N.; Betzel, C.;
Journal Biochemical and Biophysical Research Communications
Year 2006
Department PROTEOM;
Volume 344
Issue 2
Language englisch;
Keywords Prion protein; Proteinase; Proteolysis; Protein misfolding; Dynamic light scattering; Structural transformation
Abstract The transformation of the cellular prion protein (PrPC) into the infectious form (PrPSc) is implicated in the invariably fatal transmissible spongiform encephalopathies. To identify a mechanism to prevent the undesired PrPC ? PrPSc transformation, we investigated the interactions of recombinant prion proteins with a number of potential therapeutic agents which inhibit the PrPSc formation, infectivity, and the accumulation of the misfolded form. We show that the prion aggregates formed in the presence of six compounds have no ß-structure, which is typical of the infectious form, and possess considerably higher a-helical content than the normal PrPC. The investigated compounds stimulate the formation of a-helices and the destruction of ß-structure. They prevent the transformation of a-helical structure into ß-sheets. Probably, this is the reason for the resistance to PrPC ? PrPSc transformation in the presence of these compounds. The results may be useful for the future therapy of neurodegenerative diseases.
ID 2632
Persistent UFZ Identifier
Georgieva, D., Schwark, D., von Bergen, M., Redecke, L., Genov, N., Betzel, C. (2006):
Interactions of recombinant prions with compounds of therapeutical significance
Biochem. Biophys. Res. Commun. 344 (2), 463 - 470