Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides

Alejandra Alvarez, Francisca Bronfman, Cristián A. Pérez, Matías Vicente, Jorge Garrido, Nibaldo C. Inestrosa

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

64 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)49-52
Número de páginas4
PublicaciónNeuroscience Letters
Volumen201
N.º1
DOI
EstadoPublicada - 1 dic. 1995
Publicado de forma externa

Áreas temáticas de ASJC Scopus

  • Neurociencias General

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