Evidence map›Paper›PMID 33450121›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Cys-Cys and Cys-Lys Stapling of Unprotected Peptides Enabled by Hypervalent Iodine Reagents.

Javier Ceballos, Elija Grinhagena, Gontran Sangouard, Christian Heinis, Jerome Waser

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Non-symmetric stapling of native peptides.Nature reviews. Chemistry · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Recent progress in alkynylation with hypervalent iodine reagents.Chemical communications (Cambridge, England) · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Hypervalent Iodine-Mediated Late-Stage Peptide and Protein Functionalization.Angewandte Chemie (International ed. in English) · 2022
    Review
  17. Peptide stapling by late-stage Suzuki-Miyaura cross-coupling.Beilstein journal of organic chemistry · 2022
    Article
  18. Article
  19. Article
  20. 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

5 authors.

Javier CeballosLaboratory of Catalysis and Organic Synthesis, Ecole Polytechnique Fédérale de Lausanne, EPFL SB ISIC LCSO, BCH 1402, 1015, Lausanne, Switzerland.
Elija GrinhagenaLaboratory of Catalysis and Organic Synthesis, Ecole Polytechnique Fédérale de Lausanne, EPFL SB ISIC LCSO, BCH 1402, 1015, Lausanne, Switzerland.
Gontran SangouardLaboratory of Therapeutic Proteins and Peptides, Ecole Polytechnique Fédérale de Lausanne, EPFL SB ISIC LPPT, BCH 5305, 1015, Lausanne, Switzerland.
Christian HeinisLaboratory of Therapeutic Proteins and Peptides, Ecole Polytechnique Fédérale de Lausanne, EPFL SB ISIC LPPT, BCH 5305, 1015, Lausanne, Switzerland.ORCID 0000-0001-9982-9457
Jerome WaserLaboratory of Catalysis and Organic Synthesis, Ecole Polytechnique Fédérale de Lausanne, EPFL SB ISIC LCSO, BCH 1402, 1015, Lausanne, Switzerland.ORCID 0000-0002-4570-914X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Easy access to a wide range of structurally diverse stapled peptides is crucial for the development of inhibitors of protein-protein interactions. Herein, we report bis-functional hypervalent iodine reagents for two-component cysteine-cysteine and cysteine-lysine stapling yielding structurally diverse thioalkyne linkers. This stapling method works with unprotected natural amino acid residues and does not require pre-functionalization or metal catalysis. The products are stable to purification and isolation. Post-stapling modification can be accessed via amidation of an activated ester, or via cycloaddition onto the formed thioalkyne group. Increased helicity and binding affinity to MDM2 was obtained for a i,i+7 stapled peptide.

Indexed as

CysteineIndicators and ReagentsIodineLysineMolecular StructurePeptidesCysteineIndicators and ReagentsIodineLysinePeptidesbioconjugationhelicityhypervalent iodine reagentslate-stage functionalizationpeptide stapling

Identifiers

PMID33450121
PMCPMC8048981

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.