Evidence map›Paper›PMID 32893423›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Site-Selective Modification of Peptides and Proteins via Interception of Free-Radical-Mediated Dechalcogenation.

Rhys C Griffiths, Frances R Smith, Jed E Long, Huw E L Williams, Robert Layfield, Nicholas J Mitchell

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Peptide macrocyclisationChemical science · 2024
    Article
  10. Photoredox Nucleophilic (Radio)fluorination of Alkoxyamines.Journal of the American Chemical Society · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Site-Selective Installation of NAngewandte Chemie (International ed. in English) · 2022
    Article
  18. 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

6 authors.

Rhys C GriffithsSchool of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
Frances R SmithSchool of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
Jed E LongSchool of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
Huw E L WilliamsBiodiscovery Institute, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.ORCID 0000-0002-2623-6287
Robert LayfieldSchool of Life Sciences, University of Nottingham, University Park, Nottingham, NG7 2UH, UK.ORCID 0000-0003-0702-3259
Nicholas J MitchellSchool of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.ORCID 0000-0002-9041-1852

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of site-selective chemistry targeting the canonical amino acids enables the controlled installation of desired functionalities into native peptides and proteins. Such techniques facilitate the development of polypeptide conjugates to advance therapeutics, diagnostics, and fundamental science. We report a versatile and selective method to functionalize peptides and proteins through free-radical-mediated dechalcogenation. By exploiting phosphine-induced homolysis of the C-Se and C-S bonds of selenocysteine and cysteine, respectively, we demonstrate the site-selective installation of groups appended to a persistent radical trap. The reaction is rapid, operationally simple, and chemoselective. The resulting aminooxy linker is stable under a variety of conditions and selectively cleavable in the presence of a low-oxidation-state transition metal. We have explored the full scope of this reaction using complex peptide systems and a recombinantly expressed protein.

Indexed as

bioconjugationdeselenizationdesulfurizationpeptidesradical reactions

Identifiers

PMID32893423
PMCPMC7756370

What OpenQuestion holds

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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.