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A Small-Molecule Inhibitor of Prion Replication and Mutant Prion Protein Toxicity
Tania Massignan1, Valeria Sangiovanni1, Silvia Biggi1
1Dulbecco Telethon Laboratory of Prions and Amyloids, Centre for Integrative Biology, CIBIO, University of Trento, 38123, Trento, Italy.
Abstract:
Into the fold: Prion diseases are neurodegenerative disorders characterized by the accumulation in the brain of a self-replicating, misfolded isoform (PrPSc ) of the cellular prion protein (PrPC ). No therapies are available for these pathologies. We capitalized on previously described cell-based assays to screen a library of small molecules, and identified 55, a compound capable of counteracting both prion replication and toxicity. Compound 55 may represent the starting point for the development of a completely new class of therapeutics for prion diseases.
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