The toxic conformation of the 42-residue amyloid beta peptide and its relevance to oxidative stress in Alzheimer's disease.
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.
Irie
K
K
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
Murakami
K
K
Masuda
Y
Y
Morimoto
A
A
Ohigashi
H
H
Hara
H
H
Ohashi
R
R
Takegoshi
K
K
Fukuda
H
H
Nagao
M
M
Shimizu
T
T
Shirasawa
T
T
D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D000818:Animals; D016657:Cerebral Amyloid Angiopathy / Q000209:etiology / Q000378:metabolism; D005609:Free Radicals / Q000378:metabolism* / Q000633:toxicity; D006801:Humans; D020258:Neurotoxicity Syndromes / Q000209:etiology / Q000378:metabolism; D018384:Oxidative Stress; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D017434:Protein Structure, Tertiary
D016229:Amyloid beta-Peptides; D005609:Free Radicals; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)