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Atomic Insights into Amyloid-Induced Membrane Damage.

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  • 1Department of Physics, New Jersey Institute of Technology, Newark, New Jersey 07102-1982, United States.

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Summary

Amphipathic peptides damage membranes by forming pores or dissolving lipids. All-atom simulations reveal how peptide self-assembly into β-sheets drives these distinct membrane damage mechanisms.

Keywords:
amyloiddetergent-like effectlipid membranemembrane damageporation

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Area of Science:

  • Biophysics
  • Computational Biology
  • Membrane Biophysics

Background:

  • Amphipathic peptides interact with biological membranes, leading to membrane damage.
  • Mechanisms include lipid dissolution (detergent-like) and pore formation.
  • These mechanisms are relevant to amyloid peptide toxicity and antimicrobial peptide activity.

Purpose of the Study:

  • To investigate the self-assembly of membrane-bound amphipathic peptides into β-sheets.
  • To elucidate the distinct mechanisms of membrane damage (pore formation vs. lipid dissolution) at an atomic level.
  • To analyze the role of peptide-lipid interactions in membrane disruption.

Main Methods:

  • Performed all-atom molecular dynamics simulations of membrane-bound amphipathic peptides.
  • Simulated peptide self-assembly into β-sheets on and within lipid bilayers.
  • Analyzed peptide-lipid interactions and structural changes in the membrane.

Main Results:

  • Observed self-assembly of peptides into β-sheets, leading to either pore formation or lipid extrusion.
  • Strong interactions between lipid acyl tails and non-polar peptide side chains drive lipid dissolution.
  • Peptide β-sheets twist and penetrate the membrane, facilitating pore formation by connecting opposite leaflets.

Conclusions:

  • All-atom simulations provide atomic-level insights into peptide-induced membrane damage mechanisms.
  • Peptide self-assembly into β-sheets dictates whether pores form or lipids are dissolved.
  • Fibril-like structures cause minimal membrane damage due to reduced interaction with lipid tails.