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A coarse-grained model for peptide aggregation on a membrane surface.

Alex Morriss-Andrews1, Frank L H Brown, Joan-Emma Shea

  • 1Department of Physics, University of California Santa Barbara , Santa Barbara, California 93106, United States.

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Peptides form beta-rich fibrils on lipid bilayers, unlike in solution. The membrane surface influences peptide aggregation and alters local bilayer properties.

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Materials Science

Background:

  • Peptide aggregation is implicated in various diseases.
  • Understanding peptide-membrane interactions is crucial for biological and therapeutic applications.
  • Membrane environments can significantly influence peptide self-assembly.

Purpose of the Study:

  • To investigate peptide aggregation and fibril formation on a lipid bilayer surface.
  • To compare peptide self-assembly on a membrane versus a solid surface.
  • To determine the impact of aggregated fibrils on lipid bilayer properties.

Main Methods:

  • Coarse-grained molecular dynamics simulations.
  • Implicit solvent model.
  • Analysis of peptide aggregation pathways and final structures.
  • Assessment of lipid bilayer structural and mechanical changes.

Main Results:

  • Peptides self-assemble into beta-rich fibrillar aggregates on the lipid bilayer surface.
  • Membrane surface enhances peptide mobility and leads to diverse morphology transitions compared to bulk solution.
  • Aggregate structures on the membrane differ from those on a solid surface.
  • Fibrils locally alter bilayer structure and material properties but minimally affect overall bending rigidity.

Conclusions:

  • Lipid bilayers promote the formation of ordered peptide aggregates, distinct from solution behavior.
  • Membrane-induced peptide aggregation modifies local membrane properties.
  • The study provides insights into peptide-membrane interactions and their structural consequences.