ArticleBiophysical journal2016
Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous Insertion.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Antimicrobial peptide resistance in Salmonella AMR: the role of surface binding and lipopolysaccharide remodelling: one health implications.World journal of microbiology & biotechnology · 2026Review
- Melittin can permeabilize membranes via large transient pores.Nature communications · 2024Article
- The conformational properties of alamethicin in ethanol studied by NMR.European biophysics journal : EBJ · 2024Article
- Structure, Function, and Physicochemical Properties of Pore-forming Antimicrobial Peptides.Current pharmaceutical biotechnology · 2024Review
- SARS-CoV-2 fusion peptide sculpting of a membrane with insertion of charged and polar groups.Structure (London, England : 1993) · 2023Article
- Multi-oligomeric states of alamethicin ion channel: Assemblies and conductance.Biophysical journal · 2023Article
- Peptaibol Production and Characterization fromJournal of fungi (Basel, Switzerland) · 2022Article
- Dynorphin A induces membrane permeabilization by formation of proteolipidic pores. Insights from electrophysiology and computational simulations.Computational and structural biotechnology journal · 2022Article
- Predicting Membrane-Active Peptide Dynamics in Fluidic Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Spontaneous transmembrane pore formation by short-chain synthetic peptide.Biophysical journal · 2021Article
- Structure Changes of a Membrane Polypeptide under an Applied Voltage Observed with Surface-Enhanced 2D IR Spectroscopy.The journal of physical chemistry letters · 2021Article
- Tuning of a Membrane-Perforating Antimicrobial Peptide to Selectively Target Membranes of Different Lipid Composition.The Journal of membrane biology · 2021Article
- Article
- Continuum Models of Membrane Fusion: Evolution of the Theory.International journal of molecular sciences · 2020Review
- Self-Association of Antimicrobial Peptides: A Molecular Dynamics Simulation Study on Bombinin.International journal of molecular sciences · 2019Article
- Accelerated Molecular Dynamics Applied to the Peptaibol Folding Problem.International journal of molecular sciences · 2019Article
- Molecular Dynamics Simulations of Membrane Permeability.Chemical reviews · 2019Review
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
- Folding a viral peptide in different membrane environments: pathway and sampling analyses.Journal of biological physics · 2018Article
- Antimicrobial Peptides in the Cross Hairs of Computer Simulations.Biophysical journal · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
An all-atom molecular dynamics simulation of the archetype barrel-stave alamethicin (alm) pore in a 1,2-dioleoyl-sn-glycero-3-phosphocholine bilayer at 313 K indicates that ∼7 μs is required for equilibration of a preformed 6-peptide pore; the pore remains stable for the duration of the remaining 7 μs of the trajectory, and the structure factors agree well with experiment. A 5 μs simulation of 10 surface-bound alm peptides shows significant peptide unfolding and some unbinding, but no insertion. Simulations at 363 and 413 K with a -0.2 V electric field yield peptide insertion in 1 μs. Insertion is initiated by the folding of residues 3-11 into an α-helix, and mediated by membrane water or by previously inserted peptides. The stability of five alm pore peptides at 413 K with a -0.2 V electric field demonstrates a significant preference for a transmembrane orientation. Hence, and in contrast to the cationic antimicrobial peptide described in the following article, alm shows a strong preference for the inserted over the surface-bound state.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.