Conformational epitopes exposed on misfolded toxic forms of amyloid-beta, tau and alpha-synuclein directly contribute to their seeding activity.

Small misfolded regions (conformational epitopes) exposed on misfolded toxic proteins can, on their own, replicate the seeding activity of the full-length protein suggesting that they contribute to its prion-like pathogenicity. These results also indicate that these conformational epitopes represent a biologically relevant target for therapeutic antibodies.