ArticleBiochimica et biophysica acta2010
Antimicrobial peptides in toroidal and cylindrical pores.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Antimicrobial peptides in anti-infective and immunomodulatory applications: Mechanisms, challenges, and emerging computational design.Zoological research · 2026Review
- Antimicrobial Peptides and ESKAPEE Pathogens: A New Frontier in the Fight Against Antimicrobial Resistance.Probiotics and antimicrobial proteins · 2026Review
- Membrane Pore Formation Unveiled by ∞RETIS Path Sampling: From Thinning to Flip-Flop.Journal of chemical theory and computation · 2026Article
- Antimycobacterial peptides as natural therapeutics for tuberculosis: mechanisms and structural features.Frontiers in antibiotics · 2026Review
- Elucidating the Impact of Red Blood Cell Membrane Components on Melittin-Induced Pore Formation with Molecular Dynamics Simulations.The journal of physical chemistry. B · 2025Article
- Antimicrobial cyclic peptides effectively inhibit multiple forms of Borrelia and cross the blood-brain barrier model.Scientific reports · 2025Article
- Antimicrobial peptides: natural templates for next-generation therapeutics against antimicrobial resistance.Frontiers in cellular and infection microbiology · 2025Review
- Failure or future? Exploring alternative antibacterials: a comparative analysis of antibiotics and naturally derived biopolymers.Frontiers in microbiology · 2025Review
- Anticancer potentiality of Hottentotta saulcyi scorpion curd venom against breast cancer: an in vitro and in vivo study.Scientific reports · 2024Article
- Structural basis of closed groove scrambling by a TMEM16 protein.Nature structural & molecular biology · 2024Article
- Determining the Effect of Non-Thermal Plasma on the Transmembrane Kinetics of Melittin through Molecular Explorations.Biomolecules · 2024Article
- Intestinal biofilms: pathophysiological relevance, host defense, and therapeutic opportunities.Clinical microbiology reviews · 2024Review
- A promising antifungal lipopeptide from Bacillus subtilis: its characterization and insight into the mode of action.Applied microbiology and biotechnology · 2024Article
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Structural basis of closed groove scrambling by a TMEM16 protein.Research square · 2023Article
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- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Vectorial insertion of a β-helical peptide into membrane: a theoretical study on polytheonamide B.Biophysical journal · 2021Article
- Mechanistic Understanding from Molecular Dynamics in Pharmaceutical Research 2: Lipid Membrane in Drug Design.Pharmaceuticals (Basel, Switzerland) · 2021Review
4 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
Abstract
Antimicrobial peptides (AMPs) are small, usually cationic peptides, which permeabilize biological membranes. Their mechanism of action is still not well understood. Here we investigate the preference of alamethicin and melittin for pores of different shapes, using molecular dynamics (MD) simulations of the peptides in pre-formed toroidal and cylindrical pores. When an alamethicin hexamer is initially embedded in a cylindrical pore, at the end of the simulation the pore remains cylindrical or closes if glutamines in the N-termini are not located within the pore. On the other hand, when a melittin tetramer is embedded in toroidal pore or in a cylindrical pore, at the end of the simulation the pore is lined both with peptides and lipid headgroups, and, thus, can be classified as a toroidal pore. These observations agree with the prevailing views that alamethicin forms barrel-stave pores whereas melittin forms toroidal pores. Both alamethicin and melittin form amphiphilic helices in the presence of membranes, but their net charge differs; at pH approximately 7, the net charge of alamethicin is -1 whereas that of melittin is +5. This gives rise to stronger electrostatic interactions of melittin with membranes than those of alamethicin. The melittin tetramer interacts more strongly with lipids in the toroidal pore than in the cylindrical one, due to more favorable electrostatic interactions.
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