Differing modes of interaction between monomeric Aβ 1-40 peptides and model lipid membranes: An AFM study

Khizar Sheikh*, Cristiano Giordani, Jennifer J. McManus, Mads Bruun Hovgaard, Suzanne P. Jarvis

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

11 Citations (Scopus)

Abstract

Membrane interactions with β-amyloid peptides are implicated in the pathology of Alzheimer's disease and cholesterol has been shown to be key modulator of this interaction, yet little is known about the mechanism of this interaction. Using atomic force microscopy, we investigated the interaction of monomeric Aβ 1-40 peptides with planar mica-supported bilayers composed of DOPC and DPPC containing varying concentrations of cholesterol. We show that below the bilayer melting temperature, Aβ monomers adsorb to, and assemble on, the surface of DPPC bilayers to form layers that grow laterally and normal to the bilayer plane. Above the bilayer melting temperature, we observe protofibril formation. In contrast, in DOPC bilayers, Aβ monomers exhibit a detergent-like action, forming defects in the bilayer structure. The kinetics of both modes of interaction significantly increases with increasing membrane cholesterol content. We conclude that the mode and rate of the interaction of Aβ monomers with lipid bilayers are strongly dependent on lipid composition, phase state and cholesterol content.

Original languageEnglish
Pages (from-to)142-150
Number of pages9
JournalChemistry and Physics of Lipids
Volume165
Issue number2
DOIs
Publication statusPublished - 1 Feb 2012

Keywords

  • β-Amyloid peptide
  • Atomic force microscopy
  • Cholesterol
  • DOPC
  • DPPC
  • Model phospholipid membranes

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