ArticleBiophysical journal2018
Membrane Elastic Deformations Modulate Gramicidin A Transbilayer Dimerization and Lateral Clustering.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Gramicidin A in Asymmetric Lipid Membranes.Biomolecules · 2024Article
- Alteration of Average Thickness of Lipid Bilayer by Membrane-Deforming Inclusions.Biomolecules · 2023Article
- Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration.Nature communications · 2022Article
- Article
- Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides.Membranes · 2022Article
- Regulation of Antimicrobial Peptide Activity via Tuning Deformation Fields by Membrane-Deforming Inclusions.International journal of molecular sciences · 2021Article
- Peptide-induced membrane elastic deformations decelerate gramicidin dimer-monomer equilibration.Biophysical journal · 2021Article
- Quantitative Analysis of the Membrane Affinity of Local Anesthetics Using a Model Cell Membrane.Membranes · 2021Article
- Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels.Membranes · 2020Article
- Ectodomain Pulling Combines with Fusion Peptide Inserting to Provide Cooperative Fusion for Influenza Virus and HIV.International journal of molecular sciences · 2020Article
- Continuum Models of Membrane Fusion: Evolution of the Theory.International journal of molecular sciences · 2020Review
- Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting.Scientific reports · 2020Article
- Tuning ion channel mechanosensitivity by asymmetry of the transbilayer pressure profile.Biophysical reviews · 2018Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gramicidin A (gA) is a short β-helical peptide known to form conducting channels in lipid membranes because of transbilayer dimerization. The gA conducting dimer, being shorter than the lipid bilayer thickness, deforms the membrane in its vicinity, and the bilayer elastic energy contributes to the gA dimer formation energy. Likewise, membrane incorporation of a gA monomer, which is shorter than the lipid monolayer thickness, creates a void, thereby forcing surrounding lipid molecules to tilt to fill it. The energy of membrane deformation was calculated in the framework of the continuum elasticity theory, taking into account splay, tilt, lateral stretching/compression, Gaussian splay deformations, and external membrane tension. We obtained the interaction energy profiles for two gA monomers located either in the same or in the opposite monolayers. The profiles demonstrated the long-range attraction and short-range repulsion behavior of the monomers resulting from the membrane deformation. Analysis of the profile features revealed conditions under which clusters of gA monomers would not dissipate because of diffusion. The calculated dependence of the dimer formation and decay energy barriers on the membrane elastic properties was in good agreement with the available experimental data and suggested an explanation for a hitherto contentious phenomenon.
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