Evidence map›Paper›PMID 29376372›Full record

ArticleThe journal of physical chemistry. B2018

Selectivity and Mechanism of Fengycin, an Antimicrobial Lipopeptide, from Molecular Dynamics.

Sreyoshi Sur, Tod D Romo, Alan Grossfield

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

56 citing papers in PubMed, 120 citations in OpenAlex.

  1. Phenotypic and Genomic Analysis of Swine-DerivedAnimals : an open access journal from MDPI · 2026
    Article
  2. Role of C17 fengycin B fromApplied and environmental microbiology · 2026
    Article
  3. Article
  4. Lipopeptides fromBiotech (Basel (Switzerland)) · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Antimicrobial Activity ofInternational journal of molecular sciences · 2025
    Review
  10. Article
  11. From genome to field:Current research in microbial sciences · 2025
    Article
  12. Secondary Metabolites fromCurrent research in microbial sciences · 2025
    Review
  13. Genomic Characterization ofMicroorganisms · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Biocontrol of Peach Gummosis byJournal of microbiology and biotechnology · 2024
    Article
  19. Article
  20. Article
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 1 country.

Sreyoshi SurDepartment of Chemistry, University of Rochester , 404 Hutchison Hall, Box 270216, Rochester, New York 14627, United States.ORCID 0000-0001-7780-2640
Tod D RomoCenter for Integrated Research Computing, University of Rochester , 601 Elmwood Avenue, Box 712, Rochester, New York 14642, United States.
Alan GrossfieldDepartment of Biochemistry and Biophysics, University of Rochester Medical Center , Rochester, 601 Elmwood Avenue, Box 712, New York 14642, United States.
University of Rochester · USUniversity of Rochester Medical Center · US

Funding

Multiscale modeling of G protein-coupled receptorsR01GM095496 · NIGMS · UNIVERSITY OF ROCHESTER · PI GROSSFIELD, ALAN · 2011 to 2015
$1.3M
NIGMS NIH HHS R01 GM095496
6 · The paper itself

Abstract

Fengycin is a cyclic lipopeptide used as an agricultural fungicide. It is synthesized by Bacillus subtilis as an immune response against fungal infection and functions by damaging the target's cell membrane. Previous molecular dynamics simulations and experiments have led to the hypothesis that the aggregation of fengycins on the membrane surface plays a key role in cell disruption. Here, we used microsecond-scale all-atom molecular dynamics simulations to understand the specificity, selectivity, and structure of fengycin oligomers. Our simulations suggest that fengycin is more likely to form stable oligomers in model fungal membranes (phosphatidylcholine) compared to the model bacterial membranes (phosphatidylethanolamine:phosphatidylglycerol). Furthermore, we characterize the differences in the structure and kinetics of the membrane-bound aggregates and discuss their functional implications.

Indexed as

Molecular Dynamics SimulationBacillus subtilisLipopeptidesfengycinLipopeptides

Identifiers

PMID29376372
PMCPMC5832627
OpenAlexW2784348652

What OpenQuestion holds

Textmetadata
LicenceTDM
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.