Licensing opportunity
Swiss scientists have developed prion protein aggregates that mimic toxic those associated with neurodegenerative diseases such as transmissible spongiform encephalopathies (for example, Creutzfeldt-Jakob disease and BSE), Parkinson’s disease and Alzheimer’s disease. The technique, which can be used as an in vitro diagnostic tool for degenerative diseases, is now available for licensing.
Whether prion protein aggregates cause disease depends on how they replicate: the toxic scrapie form, PrPSc, results from a refolding of the cellular prion protein form, PrPC. The ETH method induces recombinant PrPC prion proteins to change conformation into PrP-beta aggregates as a result of a three-step process involving heating of lamellar lipidic structures with recombinant prion proteins in water, allowing oligomeric β-sheet formation and destroying the lipid structures – yielding what the researchers call amyloidogenic PrP-beta aggregates.
The method, which the ETH says is reproducible and accurate, avoids the use of infectious PrPSc, as its biochemical properties resemble those of PrPSc in found in fibrils and prion rods associated with scrapie. PrP-beta can be used as a quality standard and positive control for immuno-precipitation and ELISA assays.
The ETH suggests that this technology can be used not only as diagnostic tool, but also in the prevention or treatment of transmissible spongiform encephalopathies and Creutzfeldt-Jakob disease in humans.
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