ArticleBiophysical journal2013
Synergistic insertion of antimicrobial magainin-family peptides in membranes depends on the lipid spontaneous curvature.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 106 citations in OpenAlex.
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Screening and Identification of Multiple Peptides Homologous to the Fusion Glycoprotein Gc of Schmallenberg Virus Able to Inhibit Viral Infection.Transboundary and emerging diseases · 2025Article
- Binding and dimerization of PGLa peptides in anionic lipid bilayer studied by replica exchange molecular dynamics.Scientific reports · 2024Article
- Article
- Antimicrobial Peptide Synergies for Fighting Infectious Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- Magainin 2 and PGLa in bacterial membrane mimics IV: Membrane curvature and partitioning.Biophysical journal · 2022Article
- Membranolytic Mechanism of Amphiphilic Antimicrobial β-Stranded [KL]Biomedicines · 2022Article
- Probing and Manipulating the Lateral Pressure Profile in Lipid Bilayers Using Membrane-Active Peptides-A Solid-StateInternational journal of molecular sciences · 2022Article
- Magainin 2 and PGLa in bacterial membrane mimics III: Membrane fusion and disruption.Biophysical journal · 2022Article
- Membrane Interactions of Latarcins: Antimicrobial Peptides from Spider Venom.International journal of molecular sciences · 2021Article
- Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Overlapping Properties of the Short Membrane-Active Peptide BP100 With (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides.Frontiers in cellular and infection microbiology · 2021Article
- Highly synergistic antimicrobial activity of magainin 2 and PGLa peptides is rooted in the formation of supramolecular complexes with lipids.Scientific reports · 2020Article
- Chiral supramolecular architecture of stable transmembrane pores formed by an α-helical antibiotic peptide in the presence of lyso-lipids.Scientific reports · 2020Article
- Magainin 2 and PGLa in Bacterial Membrane Mimics II: Membrane Fusion and Sponge Phase Formation.Biophysical journal · 2020Article
- The Reversible Non-covalent Aggregation Into Fibers of PGLa and Magainin 2 Preserves Their Antimicrobial Activity and Synergism.Frontiers in cellular and infection microbiology · 2020Article
- Revealing the Mechanisms of Synergistic Action of Two Magainin Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- The Antimicrobial Peptide Human Beta-Defensin 2 Inhibits Biofilm Production ofFrontiers in immunology · 2020Article
- Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions.Biophysical journal · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known synergistic activity. The orientation of the two helices in membranes was studied using solid-state (15)N-NMR, for each peptide alone and for a 1:1 mixture of the peptides, in a range of different lipid systems. Two types of orientational behavior emerged. 1), In lipids with negative spontaneous curvature, both peptides remain flat on the membrane surface, when assessed both alone and in a 1:1 mixture. 2), In lipids with positive spontaneous curvature, PGLa alone assumes a tilted orientation but inserts into the bilayer in a transmembrane alignment in the presence of MAG2, whereas MAG2 stays on the surface or gets only slightly tilted, when observed both alone and in the presence of PGLa. The behavior of PGLa alone is identical to that of another antimicrobial peptide, MSI-103, in the same lipid systems, indicating that the curvature-dependent helix orientation is a general feature of membrane-bound peptides and also influences their synergistic intermolecular interactions.
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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.