[HTML][HTML] Identification of a compound that disrupts binding of amyloid-β to the prion protein using a novel fluorescence-based assay
The prion protein (PrP) has been implicated both in prion diseases such as Creutzfeldt-
Jakob disease, where its monomeric cellular isoform (PrP C) is recruited into pathogenic self-
propagating polymers of misfolded protein, and in Alzheimer disease, where PrP C may act
as a receptor for synaptotoxic oligomeric forms of amyloid-β (Aβ). There has been
considerable interest in identification of compounds that bind to PrP C, stabilizing its native
fold and thereby acting as pharmacological chaperones to block prion propagation and …
Jakob disease, where its monomeric cellular isoform (PrP C) is recruited into pathogenic self-
propagating polymers of misfolded protein, and in Alzheimer disease, where PrP C may act
as a receptor for synaptotoxic oligomeric forms of amyloid-β (Aβ). There has been
considerable interest in identification of compounds that bind to PrP C, stabilizing its native
fold and thereby acting as pharmacological chaperones to block prion propagation and …