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Related Experiment Videos

Understanding nature's design for a nanosyringe.

Carlos F Lopez1, Steve O Nielsen, Preston B Moore

  • 1Center for Molecular Modeling, Chemistry Department, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104-6323, USA. lopez@cmm.upenn.edu

Proceedings of the National Academy of Sciences of the United States of America
|April 9, 2004
PubMed
Summary

A new lipid-assisted mechanism explains how peptide assemblies insert into cell membranes. This discovery, aided by molecular dynamics simulations, reveals how lipid flips facilitate pore formation, impacting synthetic channel and antibiotic design.

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Area of Science:

  • Biophysics
  • Membrane Biology
  • Computational Chemistry

Background:

  • Peptide assemblies form nanopores for transport across biomembranes.
  • Mechanisms of membrane insertion for pore formation are not well understood.

Purpose of the Study:

  • To elucidate the fundamental mechanisms of membrane insertion for peptide assemblies.
  • To investigate the role of lipids in the passive insertion of nanotube assemblies into model membranes.

Main Methods:

  • Molecular dynamics simulations were employed.
  • A generic nanotube functionalized with hydrophilic termini was used as a model assembly.
  • A model membrane system was utilized to observe insertion dynamics.

Main Results:

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  • A lipid-assisted mechanism for passive membrane insertion was observed.
  • Transleaflet lipid flips were found to assist the assembly in crossing the membrane core.
  • Lipid tails were shown to interact with and occlude hydrophobic nanotubes.

Conclusions:

  • Lipid-assisted insertion is a key mechanism for peptide assemblies crossing biomembranes.
  • Hydrophobic-hydrophilic matching is crucial for successful membrane insertion.
  • Findings have implications for designing novel synthetic channels and antimicrobial peptides.