Evidence map›Paper›PMID 35047895›Full record

ReviewFrontiers in medical technology2020

Revealing the Mechanisms of Synergistic Action of Two Magainin Antimicrobial Peptides.

Burkhard Bechinger, Dennis Wilkens Juhl, Elise Glattard, Christopher Aisenbrey

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in medical technology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 58 citations in OpenAlex.

  1. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Antimicrobial Peptide Synergies for Fighting Infectious Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Mini-Review: Antibiotic-ResistantAntibiotics (Basel, Switzerland) · 2022
    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

4 authors at 3 institutions in 1 country.

Burkhard BechingerUniversity of Strasbourg/CNRS, UMR7177, Institut de Chimie de Strasbourg, Strasbourg, France.
Dennis Wilkens JuhlUniversity of Strasbourg/CNRS, UMR7177, Institut de Chimie de Strasbourg, Strasbourg, France.
Elise GlattardUniversity of Strasbourg/CNRS, UMR7177, Institut de Chimie de Strasbourg, Strasbourg, France.
Christopher AisenbreyUniversity of Strasbourg/CNRS, UMR7177, Institut de Chimie de Strasbourg, Strasbourg, France.
Centre National de la Recherche Scientifique · FRInstitut de Chimie de Strasbourg · FRUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of peptide-lipid and peptide-peptide interactions as well as their topology and dynamics using biophysical and structural approaches have changed our view how antimicrobial peptides work and function. It has become obvious that both the peptides and the lipids arrange in soft supramolecular arrangements which are highly dynamic and able to change and mutually adapt their conformation, membrane penetration, and detailed morphology. This can occur on a local and a global level. This review focuses on cationic amphipathic peptides of the magainin family which were studied extensively by biophysical approaches. They are found intercalated at the membrane interface where they cause membrane thinning and ultimately lysis. Interestingly, mixtures of two of those peptides namely magainin 2 and PGLa which occur naturally as a cocktail in the frog skin exhibit synergistic enhancement of antimicrobial activities when investigated together in antimicrobial assays but also in biophysical experiments with model membranes. Detailed dose-response curves, presented here for the first time, show a cooperative behavior for the individual peptides which is much increased when PGLa and magainin are added as equimolar mixture. This has important consequences for their bacterial killing activities and resistance development. In membranes that carry unsaturations both peptides align parallel to the membrane surface where they have been shown to arrange into mesophases involving the peptides and the lipids. This supramolecular structuration comes along with much-increased membrane affinities for the peptide mixture. Because this synergism is most pronounced in membranes representing the bacterial lipid composition it can potentially be used to increase the therapeutic window of pharmaceutical formulations.

Indexed as

carpet modelmembrane macroscopic phasemembrane poremembrane topologymolecular shape conceptpeptide-lipid interactionsPGLaSMART model

Identifiers

PMID35047895
PMCPMC8757784
OpenAlexW3116022174

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.