ArticleJournal of chemical theory and computation2017
Characterizing Residue-Bilayer Interactions Using Gramicidin A as a Scaffold and Tryptophan Substitutions as Probes.
Article in Journal of chemical theory and computation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Spontaneous curvature generation by peptides in asymmetric bilayers.Journal of computational chemistry · 2024Article
- Regulation of Gramicidin Channel Function Solely by Changes in Lipid Intrinsic Curvature.Frontiers in physiology · 2022Article
- Curvature Energetics Determined by Alchemical Simulation on Four Topologically Distinct Lipid Phases.The journal of physical chemistry. B · 2021Article
- Atomistic Characterization of Gramicidin Channel Formation.Journal of chemical theory and computation · 2021Article
- Molecular Mechanism for Gramicidin Dimerization and Dissociation in Bilayers of Different Thickness.Biophysical journal · 2019Article
- Quantitative Characterization of Protein-Lipid Interactions by Free Energy Simulation between Binary Bilayers.Journal of chemical theory and computation · 2019Article
- Membrane Elastic Deformations Modulate Gramicidin A Transbilayer Dimerization and Lateral Clustering.Biophysical journal · 2018Article
- Membrane Bending Moduli of Coexisting Liquid Phases Containing Transmembrane Peptide.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
Abstract
Previous experiments have shown that the lifetime of a gramicidin A dimer channel (which forms from two nonconducting monomers) in a lipid bilayer is modulated by mutations of the tryptophan (Trp) residues at the bilayer-water interface. We explore this further using extensive molecular dynamics simulations of various gA dimer and monomer mutants at the Trp positions in phosphatidylcholine bilayers with different tail lengths. gA interactions with the surrounding bilayer are strongly modulated by mutating these Trp residues. There are three principal effects: eliminating residue hydrogen bonding ability (i.e., reducing the channel-monolayer coupling strength) reduces the extent of the bilayer deformation caused by the assembled dimeric channel; a residue's size and geometry affects its orientation, leading to different hydrogen bonding partners; and increasing a residue's hydrophobicity increases the depth of gA monomer insertion relative to the bilayer center, thereby increasing the lipid bending frustration.
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Registered trials
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