The toxic conformation of the 42-residue amyloid β peptide and its relevance to oxidative stress in Alzheimer's disease

K. Irie, K. Murakami, Yuichi Masuda, A. Morimoto, H. Ohigashi, H. Hara, R. Ohashi, K. Takegoshi, H. Fukuda, M. Nagao, T. Shimizu, T. Shirasawa

Research output: Contribution to journalReview article

25 Citations (Scopus)

Abstract

Senile plaques in the brain of patients with Alzheimer's disease mainly consist of aggregates of amyloid β peptides (Aβ42, Aβ40). Aβ42 is more neurotoxic than Aβ40. This review describes recent findings from a structural analysis of Aβ42 aggregates and discusses their relevance to neurotoxicity through the formation of radicals.

Original languageEnglish
Pages (from-to)1001-1008
Number of pages8
JournalMini-Reviews in Medicinal Chemistry
Volume7
Issue number10
DOIs
Publication statusPublished - 2007 Oct 1

Keywords

  • Alzheimer's disease
  • Amyloid β
  • Cerebral amyloid angiopathy
  • ESR
  • Neurotoxicity
  • Oxidative stress
  • Proline
  • Solid-state NMR

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery

Fingerprint Dive into the research topics of 'The toxic conformation of the 42-residue amyloid β peptide and its relevance to oxidative stress in Alzheimer's disease'. Together they form a unique fingerprint.

  • Cite this

    Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Ohashi, R., Takegoshi, K., Fukuda, H., Nagao, M., Shimizu, T., & Shirasawa, T. (2007). The toxic conformation of the 42-residue amyloid β peptide and its relevance to oxidative stress in Alzheimer's disease. Mini-Reviews in Medicinal Chemistry, 7(10), 1001-1008. https://doi.org/10.2174/138955707782110187