Evidence map›Paper›PMID 31703802›Full record

ArticleBiophysical journal2019

Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions.

Michael Pachler, Ivo Kabelka, Marie-Sousai Appavou, Karl Lohner, Robert Vácha, Georg Pabst

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Antimicrobial Peptide Synergies for Fighting Infectious Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Water is a preservative of microbes.Microbial biotechnology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Michael PachlerBiophysics Division, Institute of Molecular Biosciences, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria.
Ivo KabelkaCEITEC-Central European Institute of Technology, Masaryk University, Brno, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, Czech Republic.
Marie-Sousai AppavouJülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum, Forschungszentrum Jülich GmbH, Germany.
Karl LohnerBiophysics Division, Institute of Molecular Biosciences, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria.
Robert VáchaCEITEC-Central European Institute of Technology, Masaryk University, Brno, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, Czech Republic; Department of Condensed Matter Physics, Faculty of Science, Masaryk University, Brno, Czech Republic.
Georg PabstBiophysics Division, Institute of Molecular Biosciences, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria. Electronic address: georg.pabst@uni-graz.at.
University of Graz · ATCentral European Institute of Technology · CZForschungszentrum Jülich · DE

Funding

Austrian Science Fund FWF I 1763
6 · The paper itself

Abstract

We addressed the onset of synergistic activity of the two well-studied antimicrobial peptides magainin 2 (MG2a) and PGLa using lipid-only mimics of Gram-negative cytoplasmic membranes. Specifically, we coupled a joint analysis of small-angle x-ray and neutron scattering experiments on fully hydrated lipid vesicles in the presence of MG2a and L18W-PGLa to all-atom and coarse-grained molecular dynamics simulations. In agreement with previous studies, both peptides, as well as their equimolar mixture, were found to remain upon adsorption in a surface-aligned topology and to induce significant membrane perturbation, as evidenced by membrane thinning and hydrocarbon order parameter changes in the vicinity of the inserted peptide. These effects were particularly pronounced for the so-called synergistic mixture of 1:1 (mol/mol) L18W-PGLa/MG2a and cannot be accounted for by a linear combination of the membrane perturbations of two peptides individually. Our data are consistent with the formation of parallel heterodimers at concentrations below a synergistic increase of dye leakage from vesicles. Our simulations further show that the heterodimers interact via salt bridges and hydrophobic forces, which apparently makes them more stable than putatively formed antiparallel L18W-PGLa and MG2a homodimers. Moreover, dimerization of L18W-PGLa and MG2a leads to a relocation of the peptides within the lipid headgroup region as compared to the individual peptides. The early onset of dimerization of L18W-PGLa and MG2a at low peptide concentrations consequently appears to be key to their synergistic dye-releasing activity from lipid vesicles at high concentrations.

Indexed as

Antimicrobial Cationic PeptidesCell MembraneDimerizationLipid BilayersLipidsMagaininsMolecular Dynamics SimulationPhosphatidylethanolaminesPhosphatidylglycerolsTemperature1,2-dioleoyl-sn-glycero-3-phosphoglycerol1-palmitoyl-2-oleoylphosphatidylethanolamineAntimicrobial Cationic PeptidesLipid BilayersLipidsMagaininspeptide-Gly-Leu-amidePhosphatidylethanolaminesPhosphatidylglycerols

Identifiers

PMID31703802
PMCPMC7031808
OpenAlexW2981335931

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.