Evidence map›Paper›PMID 40301231›Full record

ArticleProbiotics and antimicrobial proteins2026

Discovery and Optimisation of Novel Bombinin-Derived Peptides from Bombina variegata against Staphylococcus aureus.

Jiachen Liu, Keyi Yao, Ruize Sun, Xiaonan Ma, Chengbang Ma, Xiaoling Chen, Yangyang Jiang, Tao Wang, Tianbao Chen, Chris Shaw and 2 more

Abstract read
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In one paragraph

Article in Probiotics and antimicrobial proteins, 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

12 authors.

Jiachen Liu *Natural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Keyi Yao *Natural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Ruize Sun *Natural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Xiaonan MaNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Chengbang MaNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Xiaoling ChenNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Yangyang JiangNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK. yangyang.jiang@qub.ac.uk.
Tao WangNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK. t.wang@qub.ac.uk.
Tianbao ChenNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Chris ShawNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Mei ZhouNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.
Lei WangNatural Drug Discovery Group, School of Pharmacy, Queen's University Belfast, Belfast, Northern Ireland, BT9 7BL, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amphibian skin-secreted antimicrobial peptides (AMPs) have garnered significant attention for their excellent biological activity and low propensity for drug resistance over the past 40 years. Bombinins and bombinin H, two classes of AMPs isolated from the skin secretions of Bombina species, demonstrate strong antimicrobial activity against broad-spectrum microorganisms. In this study, two novel peptides, bombinin-like peptide 7S and bombinin-H2L, were identified from the toad, Bombina variegata. While both peptides exhibited broad-spectrum antimicrobial activity, they also showed relatively high cytotoxicity. To explore the structure-activity relationship and enhance therapeutic potential, bombinin-H2L, which displayed stronger average antimicrobial activity, was used as a template. With the aid of bioinformatics analysis, a series of bombinin-H2L analogues were designed by increasing the net positive charges and/or adjusting the amphiphilicity of the parent peptide. Among these analogues, [Arg

Indexed as

Amphibian ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesAnuraStaphylococcus aureusAnimalsBiofilmsHumansMiceMicrobial Sensitivity TestsSkinStaphylococcal InfectionsStructure-Activity RelationshipAmphibian ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesAntimicrobial peptideBiofilmsBombininDrug resistanceMembrane disruption

Identifiers

PMID40301231
PMCPMC12999879

What Socratic holds

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LicenceCC BY
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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 Socratic graph.