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

Research output: Contribution to journalArticlepeer-review

56 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)49-52
Number of pages4
JournalNeuroscience Letters
Volume201
Issue number1
DOIs
Publication statusPublished - 1 Dec 1995
Externally publishedYes

Keywords

  • Acetylcholinesterase
  • Alzheimer's disease
  • Brain G
  • Fibrillogenesis
  • Synthetic amyloid-β peptides

ASJC Scopus subject areas

  • Neuroscience(all)

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