Structure of β-amyloid fibrils and its relevance to their neurotoxicity: Implications for the pathogenesis of Alzheimer's disease

Kazuhiro Irie, Kazuma Murakami, Yuichi Masuda, Akira Morimoto, Hajime Ohigashi, Ryutaro Ohashi, Kiyonori Takegoshi, Masaya Nagao, Takahiko Shimizu, Takuji Shirasawa

Research output: Contribution to journalArticlepeer-review

78 Citations (Scopus)

Abstract

Alzheimer's disease and cerebral amyloid angiopathy are characterized by the deposition of β-amyloid fibrils consisting of 40- and 42-mer peptides (Aβ40 and Aβ42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of Aβ40 and Aβ42 fibrils have been carried out. Aβ42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of Aβ40. This review summarizes mainly our own recent findings from the structural analysis of Aβ42 fibrils and discusses its relevance to their neurotoxicity in vitro.

Original languageEnglish
Pages (from-to)437-447
Number of pages11
JournalJournal of Bioscience and Bioengineering
Volume99
Issue number5
DOIs
Publication statusPublished - 2005 May

Keywords

  • Alzheimer's disease
  • Amyloid
  • Aβ40
  • Aβ42
  • Cerebral amyloid angiopathy
  • Familial Alzheimer's disease
  • Neurotoxicity
  • Oxidative stress
  • Solid-state nuclear magnetic resonance

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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