Evidence map›Paper›PMID 42503637›Full record

ArticleJournal of medicinal chemistry2026

Dual-Mechanism Antimicrobial Peptides from a Nature-Inspired Scaffold.

Luisa I Beyer, Johannes Thoma, Silvana Lord Smits, Annie Justh de Neczpal, Hanna Mårtensson, Julia Leandersson, Maya Tabbaa, Anne Farewell, Åsa Sjöling, Alexandra Stubelius and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Luisa I BeyerUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Johannes ThomaUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.ORCID 0000-0003-3584-8274
Silvana Lord SmitsUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Annie Justh de NeczpalUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Hanna MårtenssonCenter for Antibiotic Resistance Research in Gothenburg, The University of Gothenburg, Box 100, Gothenburg405 30, Sweden.
Julia LeanderssonUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Maya TabbaaUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Anne FarewellUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Åsa SjölingUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.
Alexandra StubeliusChalmers University of Technology , Department of Life Sciences, Kemigården 4, Göteborg412 96, Sweden.
Alesia A TietzeUniversity of Gothenburg , Department of Chemistry and Molecular Biology, Medicinaregatan 16, Gothenburg413 90, Sweden.ORCID 0000-0002-9281-548X

Funding

Adlerbertska Stiftelserna NACancerfonden 25 4861G?teborgs Universitet NA?ke Wiberg Stiftelse M23-0206Knut och Alice Wallenbergs Stiftelse NASvenska S?llskapet f?r Medicinsk Forskning PD20-0191Swedish Research Council (VR) 2023-03774Swedish Research Council (VR) 2025-05306
6 · The paper itself

Abstract

Antimicrobial peptides are promising alternatives to conventional antibiotics, yet systematic strategies to enhance their potency and elucidate their mechanisms of action remain limited. Here, we generated and evaluated a focused library of 20 peptides derived from the lead peptide L3. Across clinically relevant pathogens, including Escherichia coli, Klebsiella pneumoniae, Staphylococcus aureus, and Candida albicans, several variants showed enhanced antibacterial activity, reducing MIC values to as low as 32 μg/mL (G2-4). Additional candidates (G1-8, G2-1, G2-2, G2-10) achieved MICs of 64 μg/mL against E. coli. Studies in environmental Escherichia isolates revealed species-specific susceptibility patterns. Mechanistic investigations demonstrated minimal membrane-lytic activity at concentrations exceeding their MICs, indicating that membrane disruption is not their primary mode of action. In contrast, in vitro transcription/translation assays demonstrated potent inhibition of protein expression. These results demonstrate how targeted sequence refinement can substantially enhance antimicrobial potency while modulating interactions with bacterial membranes and the transcription/translation machinery.

Indexed as

Anti-Bacterial AgentsAntimicrobial PeptidesCandida albicansEscherichia coliKlebsiella pneumoniaeMicrobial Sensitivity TestsStaphylococcus aureusStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Peptides

Identifiers

PMID42503637
PMCPMC13492378

What OpenQuestion holds

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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.