25041 Therapeutics for prion diseases
Researchers at Sheffield University have found several small drug-like molecules that interact with human PrPC (huPrPC) and/or reduce levels of PrPSc in persistently infected cells, which could be used as novel prion disease therapeutics.
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Prion diseases, or transmissible spongiform encephalopathies (TSEs), are invariably fatal neurodegenerative disorders affecting humans and animals. As yet, no effective curative or prophylactic therapy exists. Prion diseases are characterised by the accumulation of fibrils of PrPSc, the infectious and protease-resistant form of the cellular prion protein (PrPC).
Humans are susceptible to several prion diseases including Creutzfeldt-Jacob Disease (CJD), Gerstmann-Straussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI), Kuru and Alpers Syndrome. A new variant of the human TSE Creutzfeldt-Jacob disease (vCJD) was discovered, which represents a highly significant risk to public health due to transmission both to and between humans.
The formation of amyloid fibrils in prion diseases is also a feature of Alzheimer’s, Parkinson’s and Type II diabetes. Individual fibres polymerise into highly stable, insoluble cross-linked masses. These structures are toxic to cells. For prion diseases, these structures represent the infectious agent. Researchers at Sheffield University have found several small drug-like molecules that interact with human PrPC (huPrPC) and/or reduce levels of PrPSc in persistently infected cells, which could be used as novel prion disease therapeutics.
We have filed a patent application relating to the compounds and their use in therapy, especially in the treatment of prion diseases. Agents that interact with huPrPc could have application in the treatment of the following diseases:
- Creutzfeldt-Jakob disease (CJD)
- Gerstmann-Straussler-Sheinker disease
- Transmissible spongiform encephalopathies (TSE)
- Bovine spongiform encephalopathies
- Kuru
- Fatal familial insomnia
- Scrapie
- Chronic wasting disease
For further information please download the summary document below:
Outlicensingopportunity25041Therapeuticsforpriondisease.pdf