Evidence map›Paper›PMID 42372144›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Antimicrobial peptoids pass rapidly through bacterial membranes and flocculate ribosomes and DNA: A single-cell fluorescence study.

Yanyu Zhu, Josefine Eilsø Nielsen, Natalia Molchanova, Mainak Mustafi, Claudine Herlan, Bettina Fleck, Stefan Bräse, Ute Schepers, Kristian Sørensen, Claudia Zielke and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

14 authors.

Yanyu Zhu *Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706.ORCID 0000-0001-8681-976X
Josefine Eilsø Nielsen *Department of Bioengineering, Schools of Medicine and of Engineering, Stanford University, Stanford, CA 94305.
Natalia MolchanovaThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Mainak MustafiDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706.
Claudine HerlanInstitute of Biological and Chemical Systems-Functional Molecular Systems, Karlsruhe Institute of Technology, Karlsruhe 76131, Germany.
Bettina FleckInstitute of Biological and Chemical Systems-Functional Molecular Systems, Karlsruhe Institute of Technology, Karlsruhe 76131, Germany.
Stefan BräseInstitute of Biological and Chemical Systems-Functional Molecular Systems, Karlsruhe Institute of Technology, Karlsruhe 76131, Germany.
Ute SchepersInstitute of Functional Interfaces, Karlsruhe Institute of Technology, Karlsruhe 76131, Germany.
Kristian SørensenDepartment of Bioengineering, Schools of Medicine and of Engineering, Stanford University, Stanford, CA 94305.
Claudia ZielkeDepartment of Bioengineering, Schools of Medicine and of Engineering, Stanford University, Stanford, CA 94305.ORCID 0000-0003-4654-4903
Jennifer S LinDepartment of Bioengineering, Schools of Medicine and of Engineering, Stanford University, Stanford, CA 94305.ORCID 0000-0001-9169-7410
James C WeisshaarDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706.ORCID 0000-0002-0922-5113
Håvard JenssenDepartment of Science and Environment, Roskilde University, Roskilde 4000, Denmark.
Annelise E BarronDepartment of Bioengineering, Schools of Medicine and of Engineering, Stanford University, Stanford, CA 94305.ORCID 0000-0002-0735-6873

Funding

Danish Council for Independent Research 4005-00029HHS | NIH (NIH) 1DP1 OD029517HHS | NIH (NIH) R01-GM094510
6 · The paper itself

Abstract

Certain peptoids designed as mimics of host defense peptides such as LL-37 exhibit potent, broad-spectrum antibacterial, antifungal, antiparasitic, and antiviral activity with minimal cytotoxicity. Previous fixed-cell studies have suggested that the peptoids can pass through bacterial membranes and rapidly kill bacteria by aggregating intracellular macroanions, including ribosomes and DNA. However, the dynamic mechanisms of action of these biomimetic peptoids have remained elusive. We employed single-bacterial-cell, time-resolved fluorescence microscopy, and single-particle tracking methods to investigate the effects of the 12mer peptoid TM1, along with shorter alkylated and brominated analogues, on cytoplasmic membrane permeabilization and DNA and ribosome rigidification of

Indexed as

Anti-Infective AgentsAntimicrobial PeptidesCell MembraneDNA, BacterialEscherichia coliPeptoidsRibosomesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCell Membrane PermeabilityMicroscopy, FluorescenceAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesDNA, BacterialPeptoidsantibioticantimicrobial peptideantimicrobial peptoidcathelicidinLL-37

Identifiers

PMID42372144
PMCPMC13342938

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.