Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide

Raimon Sabaté, Alba Espargaró, Lucyanna Barbosa-Barros, Salvador Ventura, Joan Estelrich

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26 Citations (Scopus)

Abstract

The neurotoxicity effect of the β-amyloid (Aβ) peptide, the primary constituent of senile plaques in Alzheimer's disease, occurs through interactions with neuronal membranes. Here, we attempt to clarify the mechanisms and consequences of the interaction of Aβ with lipid membranes. We have used liposomes as a model of biological membrane, and have devoted particular attention to the bilayer charge effect. Our results show that insertion and surface association of peptide with membrane, increased in a membrane charge-dependent manner, lead to a reduction of Aβ soluble species, lag time elongation and an increase in the inter-molecular β-sheet ratio of amyloid fibrils. In addition, our findings suggest that the fine balance between peptide insertion and surface association modulates Aβ aggregation, influencing the amyloid fibrils concentration as well as their morphology. © 2012 Elsevier Masson SAS. All rights reserved.
Original languageEnglish
Pages (from-to)1730-1738
JournalBiochimie
Volume94
DOIs
Publication statusPublished - 1 Aug 2012

Keywords

  • Aggregation
  • Amyloid
  • Fibrils
  • Liposome
  • Model membrane
  • Oligomer

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