Neurotoxicity in Alzheimer's disease: is covalently crosslinked A beta responsible?
Alzheimer's disease is the most common form of dementia in the elderly, and is characterised by extracellular amyloid plaques composed of the beta-amyloid peptide (A beta). However, disease progression has been shown to correlate more closely with the level of soluble A beta oligomers. Recent evidence suggests that these oligomers are covalently crosslinked, possibly due to the interaction of A beta with redox-active metal ions. These findings offer new avenues for the treatment and prevention of disease, by modulating metal binding or preventing the formation of neurotoxic A beta oligomers.
Naylor
Ryan
R
Department of Pathology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia.
Hill
Andrew F
AF
Barnham
Kevin J
KJ
D000544:Alzheimer Disease / Q000503:physiopathology*; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D003300:Copper / Q000737:chemistry; D019281:Dimerization; D006801:Humans; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D058225:Plaque, Amyloid / Q000737:chemistry / Q000473:pathology*; D055672:Static Electricity
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D003300:Copper