Evidence map›Paper›PMID 18178659›Full record

ArticleBiophysical journal2008

Effect of fengycin, a lipopeptide produced by Bacillus subtilis, on model biomembranes.

Magali Deleu, Michel Paquot, Tommy Nylander

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

85 citing papers in PubMed, 248 citations in OpenAlex.

  1. Pathogens (Basel, Switzerland) · 2026
    Review
  2. Role of C17 fengycin B fromApplied and environmental microbiology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Cyclic lipopeptides fromFrontiers in microbiology · 2026
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Magali DeleuUnité de Chimie biologique industrielle, Faculté universitaire des Sciences agronomiques de Gembloux, B-5030 Gembloux, Belgium. deleu.m@fsagx.ac.be
Michel Paquot
Tommy Nylander
Gembloux Agro-Bio Tech · BELund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fengycin is a biologically active lipopeptide produced by several Bacillus subtilis strains. The lipopeptide is known to develop antifungal activity against filamentous fungi and to have hemolytic activity 40-fold lower than that of surfactin, another lipopeptide produced by B. subtilis. The aim of this work is to use complementary biophysical techniques to reveal the mechanism of membrane perturbation by fengycin. These include: 1), the Langmuir trough technique in combination with Brewster angle microscopy to study the lipopeptide penetration into monolayers; 2), ellipsometry to investigate the adsorption of fengycin onto supported lipid bilayers; 3), differential scanning calorimetry to determine the thermotropic properties of lipid bilayers in the presence of fengycin; and 4), cryogenic transmission electron microscopy, which provides information on the structural organization of the lipid/lipopeptide system. From these experiments, the mechanism of fengycin action appears to be based on a two-state transition controlled by the lipopeptide concentration. One state is the monomeric, not deeply anchored and nonperturbing lipopeptide, and the other state is a buried, aggregated form, which is responsible for membrane leakage and bioactivity. The mechanism, thus, appears to be driven mainly by the physicochemical properties of the lipopeptide, i.e., its amphiphilic character and affinity for lipid bilayers.

Indexed as

Membrane FluidityModels, ChemicalModels, MolecularBacillus subtilisComputer SimulationLipid BilayersLipopeptidesLipoproteinsLiposomesMembranes, ArtificialMolecular ConformationPhospholipidsfengycinLipid BilayersLipopeptidesLipoproteinsLiposomesMembranes, ArtificialPhospholipids

Identifiers

PMID18178659
PMCPMC2267117
OpenAlexW1963509429

What OpenQuestion holds

Textmetadata
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.