Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-beta-peptides
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Date
1995
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Abstract
Acetylcholinesterase (AChE) colocalizes with amyloid-beta peptide (A beta) deposits present in the brain of Alzheimer's patients. Recent studies showed that A beta(1-40) Can adopt two different conformational states in solution (an amyloidogenic conformer, A beta ac, and a non-amyloidogenic conformer, A beta nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds A beta nac and accelerates amyloid formation by the same peptide. No such effect was observed with A beta ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from A beta nac into A beta ac in vitro.
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Keywords
acetylcholinesterase, brain G(4), synthetic amyloid-beta peptides, fibrillogenesis, Alzheimer's disease