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Updated: Jun 3, 2025

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Published on: October 13, 2010
Gramicidin A in Asymmetric Lipid Membranes
Oleg V Kondrashov1, Sergey A Akimov1
1Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, Russia.
Insights
Gramicidin A channel formation is significantly influenced by lipid membrane asymmetry. This asymmetry increases the gramicidin A channel
Area of Science:
- Biophysics
- Membrane Biology
- Computational Biology
Background:
- Gramicidin A is a natural antimicrobial peptide forming cation-selective ion channels.
- Channel function is defined by conducting state lifetime and monomer-dimer equilibrium.
- Dimerization induces membrane deformations.
Purpose of the Study:
- To investigate the impact of lipid membrane asymmetry on gramicidin A channel formation.
- To quantify how spontaneous curvature and lateral tension asymmetry affect channel properties.
Main Methods:
- Theoretical modeling of gramicidin A channel formation in asymmetric lipid monolayers.
- Calculation of channel lifetime and dimerization/dissociation equilibrium constants under asymmetric conditions.
Main Results:
- Lipid monolayer asymmetry, particularly spontaneous curvature and lateral tension, influences gramicidin A channel lifetime.
- Asymmetry is predicted to significantly increase the average lifetime and equilibrium constant of gramicidin A dimerization.
- These effects are relevant to plasma membranes of mammalian cells exposed to gramicidin A.
Conclusions:
- Membrane asymmetry plays a crucial role in modulating gramicidin A ion channel function.
- The findings provide insights into gramicidin A's behavior in complex biological membranes.
- The study highlights the importance of considering membrane properties in peptide channel research.
Abstract:
Gramicidin A is a natural antimicrobial peptide produced by Bacillus brevis. Its transmembrane dimer is a cation-selective ion channel. The channel is characterized by the average lifetime of the conducting state and the monomer-dimer equilibrium constant. Dimer formation is accompanied by deformations of the membrane. We theoretically studied how the asymmetry in lipid membrane monolayers influences the formation of the gramicidin A channel. We calculated how the asymmetry in the spontaneous curvature and/or lateral tension of lipid monolayers changes the channel lifetime and shifts the equilibrium constant of the dimerization/dissociation process. For the asymmetry expected to arise in plasma membranes of mammalian cells upon the addition of gramicidin A or its derivatives to the cell exterior, our model predicts a manifold increase in the average lifetime and equilibrium constant.
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