Aβ42 oligomers can seed the fibrillization of Aβ40 peptides

Abstract Aggregation of Aβ 40 and Aβ 42 are considered as pivotal players in the pathogenic mechanism of Alzheimer's disease. In this work, we applied reverse micelles formed by sodium bis(2‐ethylhexyl) sulfosuccinate (AOT) to prepare oligomeric aggregates of Aβ 40 or Aβ 42 peptides. The resultant globular aggregates were approximately 22 nm in diameter and they were capable to form mature fibrils upon self‐aggregation. Furthermore, we found that the Aβ 42 oligomeric aggregates can seed the fibrillization of Aβ 40 monomers. Solid‐state NMR results revealed that the Aβ 40 fibrils seeded by Aβ 40 or Aβ 42 oligomers adopt a similar molecular structure for the residues near the C‐terminus.