ArticleScientific reports2020
Highly synergistic antimicrobial activity of magainin 2 and PGLa peptides is rooted in the formation of supramolecular complexes with lipids.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
- Potential of Antimicrobial Peptide Synergies for Combating Infectious Diseases in Aquaculture: A Review.Animals : an open access journal from MDPI · 2026Review
- Heteroaggregation of Antimicrobial Peptides LL-37 and HNP‑1 Drives Cooperative Neutralization of Cytotoxicity.JACS Au · 2026Article
- The rise of ultrashort cationic β-peptides as promising antimicrobial therapeutics.RSC medicinal chemistry · 2025Review
- Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly.Scientific reports · 2025Article
- Emergent conformational and aggregation properties of synergistic antimicrobial peptide combinations.Nanoscale · 2024Article
- Review
- An active machine learning discovery platform for membrane-disrupting and pore-forming peptides.Physical chemistry chemical physics : PCCP · 2024Article
- Synergy between the clavanins as a weapon against multidrug-resistantRSC medicinal chemistry · 2024Article
- Article
- Antimicrobial Peptide Synergies for Fighting Infectious Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- Leaflet by Leaflet Synergistic Effects of Antimicrobial Peptides on Bacterial and Mammalian Membrane Models.The journal of physical chemistry letters · 2023Article
- Synergy between Winter Flounder antimicrobial peptides.npj antimicrobials and resistance · 2023Article
- Magainin 2 and PGLa in bacterial membrane mimics IV: Membrane curvature and partitioning.Biophysical journal · 2022Article
- Temporin B Forms Hetero-Oligomers with Temporin L, Modifies Its Membrane Activity, and Increases the Cooperativity of Its Antibacterial Pharmacodynamic Profile.Biochemistry · 2022Article
- Antimicrobial Mechanisms and Clinical Application Prospects of Antimicrobial Peptides.Molecules (Basel, Switzerland) · 2022Review
- In vitro activity of the antimicrobial peptides h-Lf1-11, MSI-78, LL-37, fengycin 2B, and magainin-2 against clinically important bacteria.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Article
- Magainin 2 and PGLa in bacterial membrane mimics III: Membrane fusion and disruption.Biophysical journal · 2022Article
- Natural Peptides Inducing Cancer Cell Death: Mechanisms and Properties of Specific Candidates for Cancer Therapeutics.Molecules (Basel, Switzerland) · 2021Review
- Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?International journal of molecular sciences · 2020Review
- Aggregation State of Synergistic Antimicrobial Peptides.The journal of physical chemistry letters · 2020Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Magainin 2 and PGLa are cationic, amphipathic antimicrobial peptides which when added as equimolar mixture exhibit a pronounced synergism in both their antibacterial and pore-forming activities. Here we show for the first time that the peptides assemble into defined supramolecular structures along the membrane interface. The resulting mesophases are quantitatively described by state-of-the art fluorescence self-quenching and correlation spectroscopies. Notably, the synergistic behavior of magainin 2 and PGLa correlates with the formation of hetero-domains and an order-of-magnitude increased membrane affinity of both peptides. Enhanced membrane association of the peptide mixture is only observed in the presence of phophatidylethanolamines but not of phosphatidylcholines, lipids that dominate bacterial and eukaryotic membranes, respectively. Thereby the increased membrane-affinity of the peptide mixtures not only explains their synergistic antimicrobial activity, but at the same time provides a new concept to increase the therapeutic window of combinatorial drugs.
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