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Influence of the membrane dipole potential on peptide binding to lipid bilayers

Huan Zhan1, Themis Lazaridis

  • 1Department of Chemistry, City College of New York/CUNY, New York, NY 10031, USA.

Biophysical Chemistry
|November 22, 2011
PubMed

Insights

The implicit membrane model IMM1 was enhanced to include membrane dipole potential. This study reveals how dipole potential influences peptide orientation and binding affinity in cell membranes.

Area of Science:

  • Biophysics
  • Computational Biology
  • Membrane Biophysics

Background:

  • The implicit membrane model (IMM1) is crucial for simulating peptide-membrane interactions.
  • Understanding how membrane properties affect peptide behavior is essential for drug design and biological studies.

Purpose of the Study:

  • To extend the IMM1 model by incorporating membrane dipole potential.
  • To investigate the impact of dipole potential on the orientation and binding affinity of various helical peptides within a membrane environment.

Main Methods:

  • Molecular dynamics simulations were performed.
  • The extended IMM1 model, including dipole potential, was applied.
  • Simulations included diverse helical peptides: alamethicin, WALP23, influenza hemagglutinin fusion peptide, HIV fusion peptide, magainin, and p25.

Main Results:

  • Membrane dipole potential significantly influences peptide orientation within the membrane.
  • Increased dipole potential generally decreases peptide binding affinity, with exceptions like the hemagglutinin fusion peptide.
  • Observed changes are attributed to interactions between dipole potential and peptide helix backbone dipoles and charged side-chains.

Conclusions:

  • The enhanced IMM1 model provides insights into peptide-membrane electrostatics.
  • Peptide insertion and charge distribution dictate sensitivity to membrane dipole potential.
  • Positively charged peptides or those inserting their N-terminus may exhibit reduced binding with higher dipole potentials.

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