Solution NMR Studies of Recombinant Aβ(1–42): From the Presence of a Micellar Entity to Residual β-Sheet Structure in the Soluble Species

摘要: Amyloid-β (Aβ) peptide is the major component found in senile plaques of Alzheimer's disease patients. The 42-residue fragment Aβ(1–42) proposed to be one most pathogenic species therein. Here, soluble were analyzed by various liquid-state NMR methods. Transient formation a micelle was observed at onset aggregation kinetics. This dissolved after approximately day. Subsequent loss this and protofibrils are route fibril formation. Consequently, suggested on an off-pathway mechanism. Furthermore, characterization NMR-observable shows that it random-coil-like entity with low propensities for four β-strands. These β-strands correlate β-strand segments Aβ fibrils. finding indicates 3D structure fibrils might already predisposed species.