Evidence map›Paper›PMID 28970915›Full record

ArticleChemical science2017

A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins.

N Ollivier, R Desmet, H Drobecq, A Blanpain, E Boll, B Leclercq, A Mougel, J Vicogne, O Melnyk

Erratum issuedAbstract read
In one paragraph

Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Amide Chemistry Enables Redox Locking of Cyclic Disulfides for Polypeptide Assembly.Angewandte Chemie (International ed. in English) · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Solid-Phase Synthesis of Megamolecules.Journal of the American Chemical Society · 2020
    Article
  12. Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

N OllivierUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
R DesmetUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
H DrobecqUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
A BlanpainUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
E BollUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
B LeclercqUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
A MougelUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.
J VicogneUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.ORCID 0000-0001-8360-7497
O MelnykUMR CNRS 8161 CNRS , Université de Lille , Institut Pasteur de Lille , 1 rue du Pr Calmette , 59021 Lille Cedex , France . Email: oleg.melnyk@ibl.cnrs.fr.ORCID 0000-0002-3863-5613

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chemical protein synthesis gives access to well-defined native or modified proteins that are useful for studying protein structure and function. The majority of proteins synthesized up to now have been produced using native chemical ligation (NCL) in solution. Although there are significant advantages to assembling large peptides or proteins by solid phase ligation, reports of such approaches are rare. We report a novel solid phase method for protein synthesis which relies on the chemistry of the acetoacetyl group and ketoxime ligation for the attachment of the peptide to the solid support, and on a tandem transoximation/rearrangement process for the detachment of the target protein. Importantly, we show that the combination of solid phase and solution ligation techniques facilitates the production of a challenging and biologically active protein made of 180 amino acids. We show also that the solid phase method enables the purification of complex peptide segments through a chemoselective solid phase capture/release approach.

Identifiers

PMID28970915
PMCPMC5609153

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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.