The pathogenesis of Alzheimer disease appears to be strongly linked to the aggregation of
amyloid-β (Aβ) peptide and, especially, formation of soluble Aβ1–42 oligomers. It was
recently demonstrated that the cellular prion protein, PrP C, binds with high affinity to these
oligomers, acting as a putative receptor that mediates at least some of their neurotoxic
effects. Here we show that the soluble (ie glycophosphatidylinositol anchor-free) prion
protein and its N-terminal fragment have a strong effect on the aggregation pathway of Aβ1 …