Evidence map›Paper›PMID 37929096›Full record

ArticleACS omega2023

Reinvestigation of the Automated Synthesis of Stoichiometrically Conjugated Antibodies to Access High Molecular Weight Payloads and Multiplexed Conjugation via an In-Solution Trans-Tagging Process.

Victor Lehot, Ondřej Lidický, Julien Most, Stéphane Erb, Igor Dovgan, Artem Osypenko, Oleksandr Koniev, Sergii Kolodych, Lenka Kotrchová, Guilhem Chaubet and 3 more

Abstract read
In one paragraph

Article in ACS omega, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Victor LehotBio-Functional Chemistry (UMR 7199), Institut du Médicament de Strasbourg, University of Strasbourg, 74 Route du Rhin, 67400 Illkirch-Graffenstaden, France.ORCID https://orcid.org/0000-0001-6557-7191
Ondřej LidickýInstitute of Macromolecular Chemistry, Czech Academy of Sciences, Heyrovského nám. 2, 162 06 Prague 6, Czechia.
Julien MostBio-Functional Chemistry (UMR 7199), Institut du Médicament de Strasbourg, University of Strasbourg, 74 Route du Rhin, 67400 Illkirch-Graffenstaden, France.
Stéphane ErbLaboratoire de Spectrométrie de Masse BioOrganique (LSMBO), Institut du Médicament de Strasbourg, Université de Strasbourg, CNRS, IPHC UMR 7178, 67000 Strasbourg, France.
Igor DovganSyndivia SAS, 8 allée Gaspard Monge, 67000 Strasbourg, France.ORCID https://orcid.org/0000-0002-1178-8118
Artem OsypenkoSyndivia SAS, 8 allée Gaspard Monge, 67000 Strasbourg, France.
Oleksandr KonievSyndivia SAS, 8 allée Gaspard Monge, 67000 Strasbourg, France.ORCID https://orcid.org/0000-0002-6722-5621
Sergii KolodychSyndivia SAS, 8 allée Gaspard Monge, 67000 Strasbourg, France.
Lenka KotrchováInstitute of Macromolecular Chemistry, Czech Academy of Sciences, Heyrovského nám. 2, 162 06 Prague 6, Czechia.
Guilhem ChaubetBio-Functional Chemistry (UMR 7199), Institut du Médicament de Strasbourg, University of Strasbourg, 74 Route du Rhin, 67400 Illkirch-Graffenstaden, France.
Sarah CianféraniLaboratoire de Spectrométrie de Masse BioOrganique (LSMBO), Institut du Médicament de Strasbourg, Université de Strasbourg, CNRS, IPHC UMR 7178, 67000 Strasbourg, France.ORCID https://orcid.org/0000-0001-6462-5112
Tomáš EtrychInstitute of Macromolecular Chemistry, Czech Academy of Sciences, Heyrovského nám. 2, 162 06 Prague 6, Czechia.ORCID https://orcid.org/0000-0001-5908-5182
Alain WagnerBio-Functional Chemistry (UMR 7199), Institut du Médicament de Strasbourg, University of Strasbourg, 74 Route du Rhin, 67400 Illkirch-Graffenstaden, France.ORCID https://orcid.org/0000-0003-3125-601X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein conjugates have found applications in a wide variety of fields, ranging from therapeutics to imaging and detection. However, robust control over the parameters of the conjugation process (such as sites and degree of conjugation) remains challenging. Previously, our group introduced Equimolar NAtive Chemical Tagging (ENACT), a method which allows for the monofunctionalization of proteins by combining an iterative low-conversion bioconjugation, an automated process, and a bioorthogonal trans-tagging reaction. However, while the automated ENACT was dimensioned to achieve monoconjugation at the mg scale, in early stage research, because of the rarity and cost of the starting materials, it is often necessary to prepare conjugates at the lower, μg, scale. Here, we introduce modified ENACT protocols, as well as a new ENACT conjugation reagent, which allow for the monofunctionalization of proteins on the micrograms scale, using minimal quantities of payload.

Identifiers

PMID37929096
PMCPMC10620776

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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.