ArticleBiophysical journal2017
Exchange of Gramicidin between Lipid Bilayers: Implications for the Mechanism of Channel Formation.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Amyloid β 1-42 Can Form Ion Channels as Small as Gramicidin in Model Lipid Membranes.Membranes · 2025Article
- Morphology Observation of Two-Dimensional Monolayers of Model Proteins on Water Surface as Revealed by Dropping Method.Bioengineering (Basel, Switzerland) · 2024Article
- Intrinsic Lipid Curvature and Bilayer Elasticity as Regulators of Channel Function: A Comparative Single-Molecule Study.International journal of molecular sciences · 2024Article
- Screening for bilayer-active and likely cytotoxic molecules reveals bilayer-mediated regulation of cell function.The Journal of general physiology · 2023Article
- Assessing the Perturbing Effects of Drugs on Lipid Bilayers Using Gramicidin Channel-BasedJournal of medicinal chemistry · 2020Article
- Transport Properties of Gramicidin A Ion Channel in a Free-Standing Lipid Bilayer Filled With Oil Inclusions.Frontiers in cell and developmental biology · 2020Article
- Molecular Mechanism for Gramicidin Dimerization and Dissociation in Bilayers of Different Thickness.Biophysical journal · 2019Article
- Gramicidin Increases Lipid Flip-Flop in Symmetric and Asymmetric Lipid Vesicles.Biophysical journal · 2019Article
- Membrane Elastic Deformations Modulate Gramicidin A Transbilayer Dimerization and Lateral Clustering.Biophysical journal · 2018Article
- Small-molecule photostabilizing agents are modifiers of lipid bilayer properties.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The canonical mechanism of gramicidin (gA) channel formation is transmembrane dimerization of nonconducting subunits that reside in opposite bilayer leaflets. The channels do not open and close; they appear and disappear due to subunit association and dissociation. Many different types of experiments support this monomer ↔ dimer mechanism. Recently, however, this mechanism was challenged, based on experiments with lipid vesicle-incorporated gA under conditions where vesicle fusion could be controlled. In these experiments, sustained channel activity was observed long after fusion had been terminated, which led to the proposal that gA single-channel current transitions result from closed-open transitions in long-lived bilayer-spanning dimers. This proposal is at odds with 40 years of experiments, but involves the key assumption that gA monomers do not exchange between bilayers. We tested the possibility of peptide exchange between bilayers using three different types of experiments. First, we demonstrated the exchange of gA between 1,2-dierucoyl-sn-glycero-3-phosphocholine (DC
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