ArticleBiophysical journal2009
Magainin 2 revisited: a test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 127 citations in OpenAlex.
- Comparative in vitro screening identifies beta-hairpin antimicrobial peptide leads against Piscirickettsia salmonis, supported by membrane-level molecular dynamics.BMC microbiology · 2026Article
- A unified model of transient poration induced by antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Relationship between antimicrobial peptides-induced cell membrane damage and bactericidal activity.Biophysical journal · 2023Article
- Single-Cell Analysis of the Antimicrobial and Bactericidal Activities of the Antimicrobial Peptide Magainin 2.Microbiology spectrum · 2022Article
- Measuring Thousands of Single-Vesicle Leakage Events Reveals the Mode of Action of Antimicrobial Peptides.Analytical chemistry · 2022Article
- Formation of β-Strand Oligomers of Antimicrobial Peptide Magainin 2 Contributes to Disruption of Phospholipid Membrane.Membranes · 2022Article
- Indolicidin revisited: biological activity, potential applications and perspectives of an antimicrobial peptide not yet fully explored.World journal of microbiology & biotechnology · 2022Review
- Switching Cytolytic Nanopores into Antimicrobial Fractal Ruptures by a Single Side Chain Mutation.ACS nano · 2021Article
- Expanding MPEx Hydropathy Analysis to Account for Electrostatic Contributions to Protein Interactions with Anionic Membranes.The Journal of membrane biology · 2021Article
- The Antibiotic Peptide Daptomycin Functions by Reorganizing the Membrane.The Journal of membrane biology · 2021Review
- The role of membrane tension in the action of antimicrobial peptides and cell-penetrating peptides in biomembranes.Biophysical reviews · 2019Review
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
- 14-Helical β-Peptides Elicit Toxicity against C. albicans by Forming Pores in the Cell Membrane and Subsequently Disrupting Intracellular Organelles.Cell chemical biology · 2019Article
- The Mechanism of Membrane Permeabilization by Peptides: Still an Enigma.Australian journal of chemistry · 2019Article
- Dimerization of Antimicrobial Peptides: A Promising Strategy to Enhance Antimicrobial Peptide Activity.Protein and peptide letters · 2019Review
- Intracellular Delivery by Membrane Disruption: Mechanisms, Strategies, and Concepts.Chemical reviews · 2018Review
- HaloTag Assay Suggests Common Mechanism of E. coli Membrane Permeabilization Induced by Cationic Peptides.ACS chemical biology · 2018Article
- Melittin-Induced Permeabilization, Re-sealing, and Re-permeabilization of E. coli Membranes.Biophysical journal · 2018Article
- Daptomycin-Phosphatidylglycerol Domains in Lipid Membranes.Langmuir : the ACS journal of surfaces and colloids · 2017Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The all-or-none kinetic model that we recently proposed for the antimicrobial peptide cecropin A is tested here for magainin 2. In mixtures of phosphatidylcholine (PC)/phosphatidylglycerol (PG) 50:50 and 70:30, release of contents from lipid vesicles occurs in an all-or-none fashion and the differences between PC/PG 50:50 and 70:30 can be ascribed mainly to differences in binding, which was determined independently and is approximately 20 times greater to PC/PG 50:50 than to 70:30. Only one variable parameter, beta, corresponding to the ratio of the rates of pore opening to pore closing, is used to fit dye release kinetics from these two mixtures, for several peptide/lipid ratios ranging from 1:25 to 1:200. However, unlike for cecropin A where it stays almost constant, beta increases five times as the PG content of the vesicles increases from 30 to 50%. Thus, magainin 2 is more sensitive to anionic lipid content than cecropin A. But overall, magainin follows the same all-or-none kinetic model as cecropin A in these lipid mixtures, with slightly different parameter values. When the PG content is reduced to 20 mol %, dye release becomes very low; the mechanism appears to change, and is consistent with a graded kinetic model. We suggest that the peptide may be inducing formation of PG domains. In either mechanism, no peptide oligomerization occurs and magainin catalyzes dye release in proportion to its concentration on the membrane in a peptide state that we call a pore. We envision this structure as a chaotic or stochastic type of pore, involving both lipids and peptides, not a well-defined, peptide-lined channel.
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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.