ArticlePLoS computational biology2016
Pore Structure and Synergy in Antimicrobial Peptides of the Magainin Family.
Article in PLoS computational biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Antimicrobial peptides in the era of resistance: integrating AI-driven design, host-microbe interactions, and nanotechnological delivery.Frontiers in microbiology · 2026Review
- Recent Advances in Therapeutic Peptides: Innovations and Applications in Treating Infections and Diseases.ACS omega · 2025Review
- Emergent conformational and aggregation properties of synergistic antimicrobial peptide combinations.Nanoscale · 2024Article
- A Critical Review of Short Antimicrobial Peptides from Scorpion Venoms, Their Physicochemical Attributes, and Potential for the Development of New Drugs.The Journal of membrane biology · 2024Review
- Effects of C-Terminal Lys-Arg Residue of AapA1 Protein on Toxicity and Structural Mechanism.Toxins · 2023Article
- Shifting archetype to nature's hidden gems: from sources, purification to uncover the nutritional potential of bioactive peptides.3 Biotech · 2023Review
- Anticancer activities of natural antimicrobial peptides from animals.Frontiers in microbiology · 2023Review
- Tilted State Population of Antimicrobial Peptide PGLa Is Coupled to the Transmembrane Potential.Journal of chemical information and modeling · 2022Article
- Recent Progress in the Discovery and Design of Antimicrobial Peptides Using Traditional Machine Learning and Deep Learning.Antibiotics (Basel, Switzerland) · 2022Review
- Membrane fluidity, composition, and charge affect the activity and selectivity of the AMP ascaphin-8.Biophysical journal · 2022Article
- Activity of Anti-Microbial Peptides (AMPs) againstBiomolecules · 2021Review
- Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Lipid interactions of an actinoporin pore-forming oligomer.Biophysical journal · 2021Article
- Tuning of a Membrane-Perforating Antimicrobial Peptide to Selectively Target Membranes of Different Lipid Composition.The Journal of membrane biology · 2021Article
- What Makes a Good Pore Former: A Study of Synthetic Melittin Derivatives.Biophysical journal · 2020Article
- Development and Characterization of the Shortest Anti-Adhesion Peptide Analogue of B49Mod1.Molecules (Basel, Switzerland) · 2020Article
- Molecular dynamics study of membrane permeabilization by wild-type and mutant lytic peptides from the non-enveloped Flock House virus.Biochimica et biophysica acta. Biomembranes · 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
- Lipid Head Group Parameterization for GROMOS 54A8: A Consistent Approach with Protein Force Field Description.Journal of chemical theory and computation · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Magainin 2 and PGLa are among the best-studied cationic antimicrobial peptides. They bind preferentially to negatively charged membranes and apparently cause their disruption by the formation of transmembrane pores, whose detailed structure is still unclear. Here we report the results of 5-9 μs all-atom molecular dynamics simulations starting from tetrameric transmembrane helical bundles of these two peptides, as well as their stoichiometric mixture, and the analog MG-H2 in DMPC or 3:1 DMPC/DMPG membranes. The simulations produce pore structures that appear converged, although some effect of the starting peptide arrangement (parallel vs. antiparallel) is still observed on this timescale. The peptides remain mostly helical and adopt tilted orientations. The calculated tilt angles for PGLa are in excellent agreement with recent solid state NMR experiments. The antiparallel dimer structure in the magainin 2 simulations resembles previously determined NMR and crystal structures. More transmembrane orientations and a larger and more ordered pore are seen in the 1:1 heterotetramer with an antiparallel helix arrangement. Insights into the mechanism of synergy between these two peptides are obtained via implicit solvent modeling of homo- and heterodimers and analysis of interactions in the atomistic simulations. This analysis suggests stronger pairwise interactions in the heterodimer than in the two homodimers.
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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.