Evidence map›Paper›PMID 39181880›Full record

ArticleNature communications2024

Proximity-driven site-specific cyclization of phage-displayed peptides.

Libby Brown, Aldrin V Vidal, Ana Laura Dias, Tiago Rodrigues, Anna Sigurdardottir, Toby Journeaux, Siobhan O'Brien, Thomas V Murray, Peter Ravn, Monika Papworth and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Advances in Cyclic Peptides Targeting G Protein-Coupled Receptors.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Advances in Proximity-Assisted Bioconjugation.Accounts of chemical research · 2025
    Review
  8. Article
  9. Article
  10. 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

11 authors.

Libby BrownYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
Aldrin V VidalYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0003-1539-1721
Ana Laura DiasInstituto de Investigação do Medicamento (iMed), Faculdade de Farmácia, Universidade de Lisboa, Lisboa, Portugal.ORCID 0000-0002-8933-0780
Tiago RodriguesInstituto de Investigação do Medicamento (iMed), Faculdade de Farmácia, Universidade de Lisboa, Lisboa, Portugal.ORCID 0000-0002-1581-5654
Anna SigurdardottirBiologics Engineering, Oncology R&D, AstraZeneca, The Discovery Centre; Cambridge Biomedical Campus, Cambridge, UK.ORCID 0000-0002-5225-397X
Toby JourneauxYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
Siobhan O'BrienBiologics Engineering, Oncology R&D, AstraZeneca, The Discovery Centre; Cambridge Biomedical Campus, Cambridge, UK.
Thomas V MurrayBiologics Engineering, Oncology R&D, AstraZeneca, The Discovery Centre; Cambridge Biomedical Campus, Cambridge, UK.ORCID 0000-0003-3019-2739
Peter RavnBiologics Engineering, Oncology R&D, AstraZeneca, The Discovery Centre; Cambridge Biomedical Campus, Cambridge, UK.
Monika PapworthBiologics Engineering, Oncology R&D, AstraZeneca, The Discovery Centre; Cambridge Biomedical Campus, Cambridge, UK.
Gonçalo J L BernardesYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK. gb453@cam.ac.uk.ORCID 0000-0001-6594-8917

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 493006134RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) 10046039
6 · The paper itself

Abstract

Cyclization provides a general strategy for improving the proteolytic stability, cell membrane permeability and target binding affinity of peptides. Insertion of a stable, non-reducible linker into a disulphide bond is a commonly used approach for cyclizing phage-displayed peptides. However, among the vast collection of cysteine reactive linkers available, few provide the selectivity required to target specific cysteine residues within the peptide in the phage display system, whilst sparing those on the phage capsid. Here, we report the development of a cyclopropenone-based proximity-driven chemical linker that can efficiently cyclize synthetic peptides and peptides fused to a phage-coat protein, and cyclize phage-displayed peptides in a site-specific manner, with no disruption to phage infectivity. Our cyclization strategy enables the construction of stable, highly diverse phage display libraries. These libraries can be used for the selection of high-affinity cyclic peptide binders, as exemplified through model selections on streptavidin and the therapeutic target αvβ3.

Indexed as

Peptide LibraryPeptides, CyclicCapsid ProteinsCyclizationCyclopropanesCysteineHumansPeptidesStreptavidinCapsid ProteinsCyclopropanesCysteinePeptide LibraryPeptidesPeptides, CyclicStreptavidin

Identifiers

PMID39181880
PMCPMC11344848

What OpenQuestion 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 OpenQuestion graph.