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

K Irie; K Murakami; Y Masuda; A Morimoto; H Ohigashi; H Hara; R Ohashi; K Takegoshi; H Fukuda; M Nagao; T Shimizu; T Shirasawa

doi:10.2174/138955707782110187

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

Mini Rev Med Chem. 2007 Oct;7(10):1001-8. doi: 10.2174/138955707782110187.

Authors

K Irie¹, K Murakami, Y Masuda, A Morimoto, H Ohigashi, H Hara, R Ohashi, K Takegoshi, H Fukuda, M Nagao, T Shimizu, T Shirasawa

Affiliation

¹ Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan. irie@kais.kyoto-u.ac.jp

PMID: 17979802
DOI: 10.2174/138955707782110187

Abstract

Senile plaques in the brain of patients with Alzheimer's disease mainly consist of aggregates of amyloid beta peptides (Abeta42, Abeta40). Abeta42 is more neurotoxic than Abeta40. This review describes recent findings from a structural analysis of Abeta42 aggregates and discusses their relevance to neurotoxicity through the formation of radicals.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Alzheimer Disease / metabolism*
Amyloid beta-Peptides / chemistry
Amyloid beta-Peptides / metabolism*
Amyloid beta-Peptides / toxicity
Animals
Cerebral Amyloid Angiopathy / etiology
Cerebral Amyloid Angiopathy / metabolism
Free Radicals / metabolism*
Free Radicals / toxicity
Humans
Neurotoxicity Syndromes / etiology
Neurotoxicity Syndromes / metabolism
Oxidative Stress*
Peptide Fragments / chemistry
Peptide Fragments / metabolism*
Peptide Fragments / toxicity
Protein Structure, Tertiary

Substances

Amyloid beta-Peptides
Free Radicals
Peptide Fragments
amyloid beta-protein (1-42)