Acetylcholinesterase (AChE) colocalizes with amyloid -β peptide (Aβ) deposits present in the brain of Alzheimer's patients. Recent studies showed that Aβ1-40 can adopt two different conformational states in solution (an amyloidogenic conformer, Aβ ac, and a non-amyloidogenic conformer, Aβ nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds Aβ nac and accelerates amyloid formation by the same peptide. No such effect was observed with Aβ ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from Aβ nac into Aβ ac in vitro.
Áreas temáticas de ASJC Scopus
- Neurociencia (todo)