ArticleThe Journal of membrane biology2015
Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.
Article in The Journal of membrane biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Mechanistic Insights into Human Defensin Antimicrobial Activity from Membrane Simulations.The Journal of membrane biology · 2026Article
- Antimicrobial Peptides: Current Status, Mechanisms of Action, and Strategies to Overcome Therapeutic Limitations.Microorganisms · 2025Review
- Structure-Antimicrobial Activity Relationships of Recombinant Host Defence Peptides Against Drug-Resistant Bacteria.Microbial biotechnology · 2025Article
- Antimicrobial Plant Peptides: Structure, Classification, Mechanism and Therapeutic Potential.Current topics in medicinal chemistry · 2025Review
- Antimicrobial Peptides: Mechanisms, Applications, and Therapeutic Potential.Infection and drug resistance · 2025Review
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- CHARMM at 45: Enhancements in Accessibility, Functionality, and Speed.The journal of physical chemistry. B · 2024Review
- Short Antimicrobial Peptide Derived from the Venom Gland Transcriptome ofAntibiotics (Basel, Switzerland) · 2023Article
- Nerve Growth Factor, Antimicrobial Peptides and Chemotherapy: Glioblastoma Combination Therapy to Improve Their Efficacy.Biomedicines · 2023Article
- Marine Antimicrobial Peptides-Based Strategies for Tackling Bacterial Biofilm and Biofouling Challenges.Molecules (Basel, Switzerland) · 2022Review
- Review
- Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide.The Journal of membrane biology · 2022Review
- Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.The Journal of membrane biology · 2020Article
- Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields.Frontiers in microbiology · 2020Review
- Protegrin-1 cytotoxicity towards mammalian cells positively correlates with the magnitude of conformational changes of the unfolded form upon cell interaction.Scientific reports · 2019Article
- Insights into Membrane Translocation of Protegrin Antimicrobial Peptides by Multistep Molecular Dynamics Simulations.ACS omega · 2018Article
- Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.The journal of physical chemistry. B · 2017Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Computational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutants.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Membrane Protein Folding & Lipid Interactions: Theory & Experiment.The Journal of membrane biology · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Previous simulations showed that the β-hairpin antimicrobial peptide (AMP) protegrin-1 can form stable octameric β-barrels and tetrameric arcs (half barrels) in both implicit and explicit membranes. Here, we extend this investigation to several AMPs of similar structure: tachyplesin, androctonin, polyphemusin, gomesin, and the retrocyclin θ-defensin. These peptides form short β-hairpins stabilized by 2-3 disulfide bonds. We also examine synthetic β-sheet peptides selected from a combinatorial library for their ability or inability to form pores in lipid membranes. When heptameric, octameric, and decameric β-barrels and tetrameric arcs of these peptides were embedded in pre-formed neutral or anionic lipid pores (i.e., pores in neutral or anionic membranes, respectively), a variety of behaviors and membrane binding energies were observed. Due to the cationic charge of the peptides, more favorable transfer energies and more stable binding were observed in anionic than neutral pores. The synthetic peptides bound very strongly and formed stable barrels and arcs in both neutral and anionic pores. The natural AMPs exhibited unfavorable or marginally favorable binding energy and kinetic stability in neutral pores, consistent with the lower hemolytic activity of some of them compared with protegrin-1. Binding to anionic pores was more favorable, but significant distortions of the barrel or arc structures were sometimes noted. These results are discussed in light of the available experimental data. The diversity of behaviors obtained makes it unlikely that the barrel and arc mechanisms are valid for the entire family of β-hairpin AMPs.
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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.