ArticleBiophysical journal2012
Influence of hydrophobic mismatch on structures and dynamics of gramicidin a and lipid bilayers.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 102 citations in OpenAlex.
- Effects of gramicidin A on the deformation, membrane permeation and membrane stability of lipid vesicles by FeEuropean biophysics journal : EBJ · 2026Article
- The multiple sclerosis drug fingolimod induces pore-like membrane defects, contributing to its antimicrobial activity.The Journal of biological chemistry · 2026Article
- Electromechanically induced membrane restructuring enables learning and memory.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Programmable Lipid Bilayer Tension-Control Apparatus for Quantitative Mechanobiology.ACS nano · 2024Article
- Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes.Nature communications · 2024Article
- Functional regulation of aquaporin dynamics by lipid bilayer composition.Nature communications · 2024Article
- Impacts of Hydrophobic Mismatch on Antimicrobial Peptide Efficacy and Bilayer Permeabilization.Antibiotics (Basel, Switzerland) · 2023Article
- Unsaturated Lipids Facilitate Partitioning of Transmembrane Peptides into the Liquid Ordered Phase.Journal of chemical theory and computation · 2023Article
- Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023Article
- Screening for bilayer-active and likely cytotoxic molecules reveals bilayer-mediated regulation of cell function.The Journal of general physiology · 2023Article
- 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
- Mechanisms underlying drug-mediated regulation of membrane protein function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Folding and misfolding of potassium channel monomers during assembly and tetramerization.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Location and Conformational Ensemble of Menaquinone and Menaquinol, and Protein-Lipid Modulations in Archaeal Membranes.The journal of physical chemistry. B · 2021Article
- Atomistic Characterization of Gramicidin Channel Formation.Journal of chemical theory and computation · 2021Article
- Membrane-Mediated Interactions Between Protein Inclusions.Frontiers in molecular biosciences · 2021Review
- A Computational Model of Protein Induced Membrane Morphology with Geodesic Curvature Driven Protein-Membrane Interface.Journal of computational physics · 2020Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 1 country.
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Abstract
Gramicidin A (gA) is a 15-amino-acid antibiotic peptide with an alternating L-D sequence, which forms (dimeric) bilayer-spanning, monovalent cation channels in biological membranes and synthetic bilayers. We performed molecular dynamics simulations of gA dimers and monomers in all-atom, explicit dilauroylphosphatidylcholine (DLPC), dimyristoylphosphatidylcholine (DMPC), dioleoylphosphatidylcholine (DOPC), and 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) bilayers. The variation in acyl chain length among these different phospholipids provides a way to alter gA-bilayer interactions by varying the bilayer hydrophobic thickness, and to determine the influence of hydrophobic mismatch on the structure and dynamics of both gA channels (and monomeric subunits) and the host bilayers. The simulations show that the channel structure varied little with changes in hydrophobic mismatch, and that the lipid bilayer adapts to the bilayer-spanning channel to minimize the exposure of hydrophobic residues. The bilayer thickness, however, did not vary monotonically as a function of radial distance from the channel. In all simulations, there was an initial decrease in thickness within 4-5 Å from the channel, which was followed by an increase in DOPC and POPC or a further decrease in DLPC and DMPC bilayers. The bilayer thickness varied little in the monomer simulations-except one of three independent simulations for DMPC and all three DLPC simulations, where the bilayer thinned to allow a single subunit to form a bilayer-spanning water-permeable pore. The radial dependence of local lipid area and bilayer compressibility is also nonmonotonic in the first shell around gA dimers due to gA-phospholipid interactions and the hydrophobic mismatch. Order parameters, acyl chain dynamics, and diffusion constants also differ between the lipids in the first shell and the bulk. The lipid behaviors in the first shell around gA dimers are more complex than predicted from a simple mismatch model, which has implications for understanding the energetics of membrane protein-lipid interactions.
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