Evidence map›Paper›PMID 29694871›Full record

ArticleBiophysical journal2018

Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.

Regina Leber, Michael Pachler, Ivo Kabelka, Irene Svoboda, Daniel Enkoller, Robert Vácha, Karl Lohner, Georg Pabst

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

  1. Article
  2. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Antimicrobial Peptide Synergies for Fighting Infectious Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors.

Regina LeberInstitute of Molecular Biosciences, Biophysics Division, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria.
Michael PachlerInstitute of Molecular Biosciences, Biophysics Division, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria.
Ivo KabelkaCentral European Institute of Technology, Brno, Czech Republic; Faculty of Science, Masaryk University, Brno, Czech Republic.
Irene SvobodaInstitute of Molecular Biosciences, Biophysics Division, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria.
Daniel EnkollerFresenius Kabi Austria GmbH, Graz, Austria.
Robert VáchaCentral European Institute of Technology, Brno, Czech Republic; Faculty of Science, Masaryk University, Brno, Czech Republic.
Karl LohnerInstitute of Molecular Biosciences, Biophysics Division, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria.
Georg PabstInstitute of Molecular Biosciences, Biophysics Division, University of Graz, NAWI Graz, Graz, Austria; BioTechMed Graz, Graz, Austria. Electronic address: georg.pabst@uni-graz.at.

Funding

Austrian Science Fund FWF I 1763
6 · The paper itself

Abstract

Mixtures of the frog peptides magainin 2 and PGLa are well-known for their pronounced synergistic killing of Gram-negative bacteria. We aimed to gain insight into the underlying biophysical mechanism by interrogating the permeabilizing efficacies of the peptides as a function of stored membrane curvature strain. For Gram-negative bacterial-inner-membrane mimics, synergism was only observed when the anionic bilayers exhibited significant negative intrinsic curvatures imposed by monounsaturated phosphatidylethanolamine. In contrast, the peptides and their mixtures did not exhibit significant activities in charge-neutral mammalian mimics, including those with negative curvature, which is consistent with the requirement of charge-mediated peptide binding to the membrane. Our experimental findings are supported by computer simulations showing a significant decrease of the peptide-insertion free energy in membranes upon shifting intrinsic curvatures toward more positive values. The physiological relevance of our model studies is corroborated by a remarkable agreement with the peptide's synergistic activity in Escherichia coli. We propose that synergism is related to a lowering of a membrane-curvature-strain-mediated free-energy barrier by PGLa that assists membrane insertion of magainin 2, and not by strict pairwise interactions of the two peptides as suggested previously.

Indexed as

Stress, MechanicalAmino Acid SequenceAnti-Bacterial AgentsBiomechanical PhenomenaCell MembraneDrug SynergismEscherichia coliMagaininsProtein MultimerizationThermodynamicsAnti-Bacterial AgentsMagainins

Identifiers

PMID29694871
PMCPMC5937145

What OpenQuestion holds

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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 OpenQuestion graph.