Evidence map›Paper›PMID 37419980›Full record

ArticleNature communications2023

Lateral membrane organization as target of an antimicrobial peptidomimetic compound.

Adéla Melcrová, Sourav Maity, Josef Melcr, Niels A W de Kok, Mariella Gabler, Jonne van der Eyden, Wenche Stensen, John S M Svendsen, Arnold J M Driessen, Siewert J Marrink and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

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  19. PreventingACS applied materials & interfaces · 2024
    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

11 authors at 2 institutions in 2 countries.

Adéla MelcrováMolecular Biophysics, Zernike Institute for Advanced Materials, Rijksuniversiteit Groningen, Groningen, the Netherlands.ORCID 0000-0001-6390-0522
Sourav MaityMolecular Biophysics, Zernike Institute for Advanced Materials, Rijksuniversiteit Groningen, Groningen, the Netherlands.
Josef MelcrMolecular Dynamics, Groningen Biomolecular Sciences & Biotechnology Institute, Rijksuniversiteit Groningen, Groningen, the Netherlands.
Niels A W de KokMolecular Microbiology, Groningen Biomolecular Sciences & Biotechnology Institute, Rijksuniversiteit Groningen, Groningen, the Netherlands.ORCID 0000-0002-0306-892X
Mariella GablerMolecular Biophysics, Zernike Institute for Advanced Materials, Rijksuniversiteit Groningen, Groningen, the Netherlands.
Jonne van der EydenMolecular Biophysics, Zernike Institute for Advanced Materials, Rijksuniversiteit Groningen, Groningen, the Netherlands.
Wenche StensenDepartment of Chemistry, UiT Arctic University of Norway, Tromsø, Norway.ORCID 0000-0002-1272-8934
John S M SvendsenDepartment of Chemistry, UiT Arctic University of Norway, Tromsø, Norway.ORCID 0000-0001-5945-6123
Arnold J M DriessenMolecular Microbiology, Groningen Biomolecular Sciences & Biotechnology Institute, Rijksuniversiteit Groningen, Groningen, the Netherlands.ORCID 0000-0001-9258-9104
Siewert J MarrinkMolecular Biophysics, Zernike Institute for Advanced Materials, Rijksuniversiteit Groningen, Groningen, the Netherlands.ORCID 0000-0001-8423-5277
Wouter H RoosMolecular Biophysics, Zernike Institute for Advanced Materials, Rijksuniversiteit Groningen, Groningen, the Netherlands. w.h.roos@rug.nl.ORCID 0000-0002-5104-0139
University of Groningen · NLUiT The Arctic University of Norway · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial resistance is one of the leading concerns in medical care. Here we study the mechanism of action of an antimicrobial cationic tripeptide, AMC-109, by combining high speed-atomic force microscopy, molecular dynamics, fluorescence assays, and lipidomic analysis. We show that AMC-109 activity on negatively charged membranes derived from Staphylococcus aureus consists of two crucial steps. First, AMC-109 self-assembles into stable aggregates consisting of a hydrophobic core and a cationic surface, with specificity for negatively charged membranes. Second, upon incorporation into the membrane, individual peptides insert into the outer monolayer, affecting lateral membrane organization and dissolving membrane nanodomains, without forming pores. We propose that membrane domain dissolution triggered by AMC-109 may affect crucial functions such as protein sorting and cell wall synthesis. Our results indicate that the AMC-109 mode of action resembles that of the disinfectant benzalkonium chloride (BAK), but with enhanced selectivity for bacterial membranes.

Indexed as

Anti-Infective AgentsPeptidomimeticsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCell MembraneMicrobial Sensitivity TestsMolecular Dynamics SimulationStaphylococcus aureusAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesPeptidomimetics

Identifiers

PMID37419980
PMCPMC10328936
OpenAlexW4383499437

What OpenQuestion 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 OpenQuestion graph.