Extensive research causally links amyloid-β peptide (Aβ) to Alzheimer's disease, although
the pathologically relevant Aβ conformation remains unclear. Aβ spontaneously aggregates
into the fibrils that deposit in senile plaques. However, recent in vivo and in vitroreports
describe a potent biological activity for oligomeric assemblies of Aβ. To consistently prepare
in vitro oligomeric and fibrillar forms of Aβ1–42, a detailed knowledge of how solution
parameters influence structure is required. This manuscript represents the first study using a …