Solid-state NMR analysis of the β-strand orientation of the protofibrils of amyloid β-protein

Takashi Doi, Yuichi Masuda, Kazuhiro Irie, Ken ichi Akagi, Youko Monobe, Takayoshi Imazawa, K. Takegoshi

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


Alzheimer's disease (AD) is caused by abnormal deposition (fibrillation) of a 42-residue amyloid β-protein (Aβ42) in the brain. During the process of fibrillation, the Aβ42 takes the form of protofibrils with strong neurotoxicity, and is thus believed to play a crucial role in the pathogenesis of AD. To elucidate the supramolecular structure of the Aβ42 protofibrils, the intermolecular proximity of the Ala-21 residues in the Aβ42 protofibrils was analyzed by 13C-13C rotational resonance experiments in the solid state. Unlike the Aβ42 fibrils, an intermolecular 13C-13C correlation was not found in the Aβ42 protofibrils. This result suggests that the β-strands of the Aβ42 protofibrils are not in an in-register parallel orientation. Aβ42 monomers would assemble to form protofibrils with the β-strand conformation, then transform into fibrils by forming intermolecular parallel β-sheets.

Original languageEnglish
Pages (from-to)458-462
Number of pages5
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2012 Nov 30
Externally publishedYes


  • Alzheimer's disease
  • Amyloid β-protein
  • Protofibrils
  • Rotational resonance
  • Solid-state NMR

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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