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Membrane-assisted Aβ40 aggregation pathways.

Fidha Nazreen Kunnath Muhammedkutty1, Huan-Xiang Zhou1,2

  • 1Department of Chemistry, University of Illinois Chicago, Chicago, IL, USA.

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Alzheimer's disease aggregation of amyloid-beta peptides is accelerated by cell membranes. This study reveals how cholesterol and GM1 ganglioside stabilize key intermediates, offering new therapeutic targets for Alzheimer's disease.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Computational Biology

Background:

  • Alzheimer's disease (AD) pathogenesis involves amyloid-beta (Aβ) peptide aggregation into toxic oligomers and fibrils.
  • Cell membranes significantly accelerate Aβ nucleation, yet mechanisms remain poorly understood.

Purpose of the Study:

  • To structurally and energetically characterize Aβ40 aggregation intermediates on cell membranes using molecular dynamics (MD) simulations.
  • To elucidate the roles of specific membrane components and Aβ residues in aggregation.

Main Methods:

  • Extensive molecular dynamics (MD) simulations were employed.
  • Analysis focused on structural and energetic properties of Aβ40 aggregation intermediates.
  • Key interactions with GM1 ganglioside and cholesterol were investigated.

Main Results:

  • GM1 ganglioside and cholesterol stabilize membrane-embedded β-sheets of Aβ40.
  • Residues Y10 and K28 facilitate the release of an oligomeric seed into solution.
  • The seed forms either open-shaped or R-shaped fibrils, stabilized by specific β-sheet interfaces.

Conclusions:

  • This study provides the first comprehensive model of membrane-assisted Aβ40 aggregation.
  • Findings offer insights into AD pathogenesis and potential therapeutic strategies.
  • The results may help rationalize disease-specific polymorphisms in amyloidogenic proteins.