Evidence map›Paper›PMID 38253659›Full record

ArticleScientific reports2024

Interaction of designed cationic antimicrobial peptides with the outer membrane of gram-negative bacteria.

Shelley He, Charles M Deber

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
11.4field-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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
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  10. Nanosystems for delivery of indolicidin peptide.Frontiers in medical technology · 2026
    Review
  11. Article
  12. Review
  13. Article
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  18. Article
  19. Antimicrobial Peptide-Peptoid Macrocycles from the Polymyxin B2 Chemical Space.Angewandte Chemie (International ed. in English) · 2025
    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

2 authors at 2 institutions in 1 country.

Shelley HeProgram in Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Charles M DeberProgram in Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada. deber@sickkids.ca.
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN-2016-05577
6 · The paper itself

Abstract

The outer membrane (OM) is a hallmark feature of gram-negative bacteria that provides the species with heightened resistance against antibiotic threats while cationic antimicrobial peptides (CAPs) are natural antibiotics broadly recognized for their ability to disrupt bacterial membranes. It has been well-established that lipopolysaccharides present on the OM are among major targets of CAP activity against gram-negative species. Here we investigate how the relative distribution of charged residues along the primary peptide sequence, in conjunction with its overall hydrophobicity, affects such peptide-OM interactions in the natural CAP Ponericin W1. Using a designed peptide library derived from Ponericin W1, we determined that the consecutive placement of Lys residues at the peptide N- or C-terminus (ex. "PonN": KKKKKKWLGSALIGALLPSVVGLFQ) enhances peptide binding affinity to OM lipopolysaccharides compared to constructs where Lys residues are interspersed throughout the primary sequence (ex. "PonAmp": WLKKALKIGAKLLPSVVKLFKGSGQ). Antimicrobial activity against multidrug resistant strains of Pseudomonas aeruginosa was similarly found to be highest among Lys-clustered sequences. Our findings suggest that while native Ponericin W1 exerts its initial activity at the OM, Lys-clustering may be a promising means to enhance potency towards this interface, thereby augmenting peptide entry and activity at the IM, with apparent advantage against multidrug-resistant species.

Indexed as

Antimicrobial Cationic PeptidesGram-Negative BacteriaAmino Acid SequenceAnti-Bacterial AgentsCluster AnalysisLipopolysaccharidesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesLipopolysaccharides

Identifiers

PMID38253659
PMCPMC10803810
OpenAlexW4391103405

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.