Evidence map›Paper›PMID 24706874›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Small cationic antimicrobial peptides delocalize peripheral membrane proteins.

Michaela Wenzel, Alina Iulia Chiriac, Andreas Otto, Dagmar Zweytick, Caroline May, Catherine Schumacher, Ronald Gust, H Bauke Albada, Maya Penkova, Ute Krämer and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.

0numbers the graph read from it
0cells of the map it votes in
141citing papers in PubMed
24.5field-weighted citation impact, top 1% 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

141 citing papers in PubMed, 337 citations in OpenAlex.

  1. Article
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  9. Contribution of theMicrobiology spectrum · 2026
    Article
  10. CLEC3A-derived peptides exhibit broad-spectrum activity againstFrontiers in cellular and infection microbiology · 2026
    Article
  11. Deep-Learning Driven Identification of Novel Antimicrobial Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. PreventingACS applied materials & interfaces · 2024
    Article

81 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

18 authors at 12 institutions in 8 countries.

Michaela WenzelBiology of Microorganisms, Bioinorganic Chemistry, and Plant Physiology, Immune Proteomics, Medical Proteome Center, and Institute of Physiological Chemistry, Ruhr University Bochum, 44801 Bochum, Germany.
Alina Iulia Chiriac
Andreas Otto
Dagmar Zweytick
Caroline May
Catherine Schumacher
Ronald Gust
H Bauke Albada
Maya Penkova
Ute Krämer
Ralf Erdmann
Nils Metzler-Nolte
Suzana K Straus
Erhard Bremer
Dörte Becher
Heike Brötz-Oesterhelt
Hans-Georg Sahl
Julia Elisabeth Bandow
University of Nariño · COG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RUHeinrich Heine University Düsseldorf · DEUniversität Greifswald · DEUniversity of Bonn · DEGeorgetown University · USPhilipps University of Marburg · DEProteome Sciences (United Kingdom) · GBRuhr University Bochum · DEUniversität Innsbruck · ATUniversity of British Columbia · CAUniversity of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Short antimicrobial peptides rich in arginine (R) and tryptophan (W) interact with membranes. To learn how this interaction leads to bacterial death, we characterized the effects of the minimal pharmacophore RWRWRW-NH2. A ruthenium-substituted derivative of this peptide localized to the membrane in vivo, and the peptide also integrated readily into mixed phospholipid bilayers that resemble Gram-positive membranes. Proteome and Western blot analyses showed that integration of the peptide caused delocalization of peripheral membrane proteins essential for respiration and cell-wall biosynthesis, limiting cellular energy and undermining cell-wall integrity. This delocalization phenomenon also was observed with the cyclic peptide gramicidin S, indicating the generality of the mechanism. Exogenous glutamate increases tolerance to the peptide, indicating that osmotic destabilization also contributes to antibacterial efficacy. Bacillus subtilis responds to peptide stress by releasing osmoprotective amino acids, in part via mechanosensitive channels. This response is triggered by membrane-targeting bacteriolytic peptides of different structural classes as well as by hypoosmotic conditions.

Indexed as

Antimicrobial Cationic PeptidesBacillus subtilisBinding SitesCytochromes cHomeostasisLipid BilayersMembrane ProteinsPhospholipidsAntimicrobial Cationic PeptidesCytochromes cLipid BilayersMembrane ProteinsPhospholipidshypoosmotic stress responsemechanism of actionmetallocenesrespiratory chain

Identifiers

PMID24706874
PMCPMC3986158
OpenAlexW2170849801

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.