Evidence map›Paper›PMID 29273729›Full record

ArticleNature communications2017

Antimicrobial peptide capsids of de novo design.

Emiliana De Santis, Hasan Alkassem, Baptiste Lamarre, Nilofar Faruqui, Angelo Bella, James E Noble, Nicola Micale, Santanu Ray, Jonathan R Burns, Alexander R Yon and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Probing theRSC chemical biology · 2026
    Article
  2. Article
  3. Measuring multisubunit mechanics of geometrically programmed colloidal assemblies via cryo-EM multi-body refinement.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. The future of recombinant host defense peptides.Microbial cell factories · 2022
    Review
  11. Article
  12. Anticancer Activity of Reconstituted Ribonuclease S-Decorated Artificial Viral Capsid.Chembiochem : a European journal of chemical biology · 2022
    Article
  13. Article
  14. Protein Nanoparticles: Uniting the Power of Proteins with Engineering Design Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Emiliana De SantisNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
Hasan AlkassemNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
Baptiste LamarreNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
Nilofar FaruquiNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
Angelo BellaNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
James E NobleNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
Nicola MicaleDipartimento di Scienze Chimiche, Biologiche, Farmaceutiche ed Ambientali, Università degli Studi di Messina, 98168, Messina, Italy.
Santanu RaySET, University of Brighton, Brighton, BN2 4GJ, UK.
Jonathan R BurnsDepartment of Chemistry, University College London, London, WC1E 6BT, UK.
Alexander R YonLondon Centre for Nanotechnology, University College London, London, WC1H 0AH, UK.
Bart W HoogenboomLondon Centre for Nanotechnology, University College London, London, WC1H 0AH, UK.ORCID http://orcid.org/0000-0002-8882-4324
Maxim G RyadnovNational Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK. max.ryadnov@npl.co.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spread of bacterial resistance to antibiotics poses the need for antimicrobial discovery. With traditional search paradigms being exhausted, approaches that are altogether different from antibiotics may offer promising and creative solutions. Here, we introduce a de novo peptide topology that-by emulating the virus architecture-assembles into discrete antimicrobial capsids. Using the combination of high-resolution and real-time imaging, we demonstrate that these artificial capsids assemble as 20-nm hollow shells that attack bacterial membranes and upon landing on phospholipid bilayers instantaneously (seconds) convert into rapidly expanding pores causing membrane lysis (minutes). The designed capsids show broad antimicrobial activities, thus executing one primary function-they destroy bacteria on contact.

Indexed as

Drug Resistance, BacterialAnti-Infective AgentsAntimicrobial Cationic PeptidesBacteriaCapsidChemistry Techniques, SyntheticChromatography, High Pressure LiquidCryoelectron MicroscopyDrug DiscoveryHumansLipid BilayersMicrobial Sensitivity TestsMicroscopy, Electron, TransmissionPhospholipidsAnti-Infective AgentsAntimicrobial Cationic PeptidesLipid BilayersPhospholipids

Identifiers

PMID29273729
PMCPMC5741663

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.