Evidence map›Paper›PMID 42162318›Full record

ArticleNature biomedical engineering2026

Modular peptide nanofibres that self-assemble on bacterial membranes overcome antimicrobial resistance.

Ziao Zhou, Dinghao Chen, Jiang Ouyang, Nan Kong, Hongyue Zhang, Laicheng Zhou, Jing Wang, Tengyan Xu, Wei Chen, Na Kong and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature biomedical engineering, 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.

Ziao Zhou *Zhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.ORCID http://orcid.org/0009-0001-3685-5946
Dinghao Chen *Zhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.ORCID http://orcid.org/0009-0000-3495-7095
Jiang Ouyang *Center for Nanomedicine and Department of Anesthesiology, Perioperative, and Pain Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.
Nan KongZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.
Hongyue ZhangZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.
Laicheng ZhouZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.
Jing WangZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.
Tengyan XuZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China.
Wei ChenCenter for Nanomedicine and Department of Anesthesiology, Perioperative, and Pain Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.
Na KongCenter for Nanomedicine and Department of Anesthesiology, Perioperative, and Pain Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.
Wei TaoCenter for Nanomedicine and Department of Anesthesiology, Perioperative, and Pain Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA. wtao@bwh.harvard.edu.ORCID http://orcid.org/0000-0002-4277-3728
Huaimin WangZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, Hangzhou, China. wanghuaimin@westlake.edu.cn.ORCID http://orcid.org/0000-0002-8796-0367

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drug-resistant bacterial infections increasingly evade available antimicrobials, and many existing antimicrobial peptides remain limited by instability, toxicity to mammalian membranes and high manufacturing cost. Here we introduce a modular peptide technology that self-assembles into nanofibres on bacterial surfaces through a membrane-anchoring biphenyl group, a diphenylalanine linker and a cationic minimalistic peptide that together enable selective disruption of drug-resistant pathogens. Using cryogenic electron microscopy, molecular dynamics simulations, lipid-nanoparticle membrane mimetics and binding thermodynamics, we show that the peptide first forms short nanofibres that dock onto phosphatidylglycerol and then elongates into nanofibres that penetrate and destabilize the bacterial membrane without inducing resistance. The nanofibres retain antibacterial activity when recycled from killed bacteria and outperform vancomycin and several classical antimicrobial peptides against dense bacterial populations in vitro. In a mouse model of methicillin-resistant Staphylococcus aureus pneumonia, inhaled peptide nanofibres eradicate pulmonary infection and restore lung architecture without detectable toxicity. This modular strategy enables the design of potent, selective and low-cost antimicrobials.

Identifiers

PMID42162318

What OpenQuestion holds

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Registered trials

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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.