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Related Experiment Videos

Membrane perturbation induced by interfacially adsorbed peptides.

Assaf Zemel1, Avinoam Ben-Shaul, Sylvio May

  • 1Department of Physical Chemistry and the Fritz Haber Research Center, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.

Biophysical Journal
|June 11, 2004
PubMed
Summary

This study models peptide-lipid interactions, revealing how peptides alter membrane structure and mediate attractive forces, promoting peptide aggregation. It also shows hydrophobic peptides prefer to insert into, rather than adsorb onto, lipid bilayers.

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Area of Science:

  • Biophysics
  • Membrane Biophysics
  • Computational Biology

Background:

  • Understanding peptide-lipid interactions is crucial for membrane protein function and drug design.
  • Lipid bilayers exhibit complex structural and dynamic properties influenced by embedded molecules.
  • Alpha-helical peptides are common membrane-associated proteins with diverse biological roles.

Purpose of the Study:

  • To investigate the structural and energetic consequences of alpha-helical, amphipathic peptide adsorption to lipid bilayers.
  • To elucidate the molecular mechanisms underlying peptide-induced membrane perturbations and inter-peptide interactions.
  • To explore the orientation preferences of hydrophobic peptides within lipid bilayers.

Main Methods:

  • A molecular-level theory of lipid chain packing in membranes was employed.

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  • Peptides were modeled as amphipathic cylinders with defined polar angles.
  • A cell-like model was used to evaluate membrane perturbation free energy under 2D nematic order.

    • Main Results:

    • Peptide adsorption causes membrane thinning and distorts lipid chain structure (stretching and bending).
    • Calculated changes in lipid bond order parameters align with magnetic resonance measurements.
    • Membrane-mediated attractive interactions between adsorbed peptides were identified, suggesting aggregation mechanisms.
    • Hydrophobic peptides show a strong preference for transmembrane insertion over surface adsorption.

    Conclusions:

    • Peptide adsorption significantly perturbs lipid bilayer structure and energetics.
    • The model provides insights into peptide aggregation on membranes.
    • Findings are consistent with experimental observations and offer a mechanistic explanation for peptide-membrane interactions.