ArticleBiophysical journal2008
Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 112 citations in OpenAlex.
- Killer bee molecules: antimicrobial peptides as effector molecules to target sporogonic stages of Plasmodium.PLoS pathogens · 2013Trial
- Membrane-Traversing Peptides: Mechanistic Landscapes, Assays, and Applications.Chemical reviews · 2026Review
- Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly.Scientific reports · 2025Article
- Design, Structural Stability, Membrane Binding, and Antibacterial Activity of Novel Antimicrobial Peptides Derived from Wuchuanin-A1.Life (Basel, Switzerland) · 2025Article
- Antimicrobial Peptides: Classification, Mechanism, and Application in Plant Disease Resistance.Probiotics and antimicrobial proteins · 2025Review
- Exploring Tryptophan-based Short Peptides: Promising Candidate for Anticancer and Antimicrobial Therapies.Anti-cancer agents in medicinal chemistry · 2025Article
- Article
- Investigation of the Mechanism of Action of AMPs from Amphibians to Identify Bacterial Protein Targets for Therapeutic Applications.Antibiotics (Basel, Switzerland) · 2024Review
- Expression and purification of epinecidin-1 variant (Ac-Var-1) by acid cleavage.Applied microbiology and biotechnology · 2024Article
- Therapeutic Potential of Antimicrobial Peptide PN5 against Multidrug-Resistant E. coli and Anti-Inflammatory Activity in a Septic Mouse Model.Microbiology spectrum · 2022Article
- Advancements in antimicrobial nanoscale materials and self-assembling systems.Chemical Society reviews · 2022Review
- Antimicrobial peptide nisin induces spherical distribution of macropinocytosis-like cytokeratin 5 and cytokeratin 17 following immediate derangement of the cell membrane.Anatomy & cell biology · 2022Article
- Lipid tails modulate antimicrobial peptide membrane incorporation and activity.Biochimica et biophysica acta. Biomembranes · 2022Article
- Anti-Pythium insidiosum activity of MSI-78, LL-37, and magainin-2 antimicrobial peptides.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Article
- Antimicrobial Peptides with Antibacterial Activity against Vancomycin-ResistantInternational journal of molecular sciences · 2021Review
- Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021Review
- Review: Examining the Natural Role of Amphibian Antimicrobial Peptide Magainin.Molecules (Basel, Switzerland) · 2020Review
- Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization.Nature communications · 2020Article
- Amyloids: Regulators of Metal Homeostasis in the Synapse.Molecules (Basel, Switzerland) · 2020Review
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions of cationic antimicrobial peptides with living bacterial and mammalian cells are little understood, although model membranes have been used extensively to elucidate how peptides permeabilize membranes. In this study, the interaction of F5W-magainin 2 (GIGKWLHSAKKFGKAFVGEIMNS), an equipotent analogue of magainin 2 isolated from the African clawed frog Xenopus laevis, with unfixed Bacillus megaterium and Chinese hamster ovary (CHO)-K1 cells was investigated, using confocal laser scanning microscopy. A small amount of tetramethylrhodamine-labeled F5W-magainin 2 was incorporated into the unlabeled peptide for imaging. The influx of fluorescent markers of various sizes into the cytosol revealed that magainin 2 permeabilized bacterial and mammalian membranes in significantly different ways. The peptide formed pores with a diameter of approximately 2.8 nm (< 6.6 nm) in B. megaterium, and translocated into the cytosol. In contrast, the peptide significantly perturbed the membrane of CHO-K1 cells, permitting the entry of a large molecule (diameter, >23 nm) into the cytosol, accompanied by membrane budding and lipid flip-flop, mainly accumulating in mitochondria and nuclei. Adenosine triphosphate and negatively charged glycosaminoglycans were little involved in the magainin-induced permeabilization of membranes in CHO-K1 cells. Furthermore, the susceptibility of CHO-K1 cells to magainin was found to be similar to that of erythrocytes. Thus, the distinct membrane-permeabilizing processes of magainin 2 in bacterial and mammalian cells were, to the best of our knowledge, visualized and characterized in detail for the first time.
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Registered trials
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