Prion protein (misfolded form, also called PrP^Sc) (PrP^Sc)

The **misfolded prion protein** (PrP^Sc) is a pathogenic, beta-sheet–rich conformational isoform of the normal cellular prion protein (PrP^C), found mainly on neuronal membranes[2][4][1]. PrP^Sc induces normal PrP^C to adopt its misfolded, aggregation-prone structure, resulting in fibrillar amyloid deposits that disrupt brain function and ultimately cause fatal neurodegeneration, characteristic of prion diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy[2][1][6]. This aberrant, self-propagating protein aggregate acts as both the disease agent and the target for experimental therapies, with current drug research focused on blocking aggregation and enhancing clearance or stabilization of native PrP. There are no approved disease-modifying drugs for prion diseases, and diagnosis relies largely on detection of PrP^Sc as a biomarker of disease progression[3][4][2].

Other names

PrP^Scscrapie prion proteinmisfolded prion proteinpathogenic prion proteininfectious prion protein

Antibodies: Binding to PrP^Sc to prevent or reverse misfolding/aggregation[3] Small molecules: Inhibition of prion aggregation, stabilization of native conformation[3]