Major prion protein (PrP)

The major prion protein (PrP), encoded by the PRNP gene, is a highly conserved glycoprotein primarily expressed in the nervous system and tethered to the cell surface via a glycosylphosphatidylinositol (GPI) anchor[1][2][4][7]. While its precise physiological function is unclear, PrP is implicated in neuroprotection, copper metabolism, and the formation and maintenance of neuronal synapses[3]. The normal cellular form, PrP^C^, can misfold into a protease-resistant conformer, PrP^Sc^, which aggregates and drives transmissible spongiform encephalopathies (prion diseases) such as Creutzfeldt–Jakob disease, kuru, and scrapie[1][3]. PrP is not an enzyme or classic receptor, but its pathological conformer is a unique causative agent for neurodegenerative disease and a high-profile drug target for rare but lethal disorders. No approved drugs with established efficacy currently exist against prion diseases, although PrP remains intensively studied for potential therapeutics and diagnostics[1][3].

Other names

PrPPrP^C^CD230Cluster of differentiation 230Prion proteinPrion protein cellular formPrP^Sc^ (for pathological form)PRIPALTPRP

Direct binding and stabilization of normal PrP conformation (investigational); Prevention of PrP^C^ to PrP^Sc^ conversion (research, experimental); Inhibition of prion aggregation (research)