Spontaneous self-assembly of amyloid β (1-40) into dimers

Mohtadin Hashemi, Yuliang Zhang, Zhengjian Lv, Yuri L. Lyubchenko

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered monomers assemble into aggregates remains largely unknown. In this work, we characterize the assembly of Aβ (1-40) monomers into dimers using long-time molecular dynamics simulations. Upon interaction, the monomers undergo conformational transitions, accompanied by change of the structure, leading to the formation of a stable dimer. The dimers are stabilized by interactions in the N-terminal region (residues 5-12), in the central hydrophobic region (residues 16-23), and in the C-terminal region (residues 30-40); with inter-peptide interactions focused around the N- and C-termini. The dimers do not contain long β-strands that are usually found in fibrils.

Original languageEnglish (US)
Pages (from-to)3892-3899
Number of pages8
JournalNanoscale Advances
Issue number10
StatePublished - 2019

ASJC Scopus subject areas

  • General Engineering
  • Bioengineering
  • Atomic and Molecular Physics, and Optics
  • General Materials Science
  • General Chemistry


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