42 oligomers can seed the fibrillization of Aβ40 peptides

Yi Shan Wu, Shing Jong Huang, Meng Hsin Wu, Ling Hsien Tu, Ming Che Lee, Jerry Chun Chung Chan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


Aggregation of Aβ40 and Aβ42 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 Aβ40 or Aβ42 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 Aβ42 oligomeric aggregates can seed the fibrillization of Aβ40 monomers. Solid-state NMR results revealed that the Aβ40 fibrils seeded by Aβ40 or Aβ42 oligomers adopt a similar molecular structure for the residues near the C-terminus.

Original languageEnglish
Pages (from-to)1318-1325
Number of pages8
JournalJournal of the Chinese Chemical Society
Issue number8
Publication statusPublished - 2022 Aug


  • beta amyloid
  • cross seeding
  • reverse micelles
  • solid-state NMR

ASJC Scopus subject areas

  • General Chemistry


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