ArticleChemical science2019
Cysteine-to-lysine transfer antibody fragment conjugation.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Site-specific labelling of native peptides and proteins: chemical and enzymatic strategies.Beilstein journal of organic chemistry · 2026Review
- Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.Chembiochem : a European journal of chemical biology · 2024Article
- Understanding the Specific Implications of Amino Acids in the Antibody Development.The protein journal · 2024Review
- The Nitrile Bis-Thiol Bioconjugation Reaction.Journal of the American Chemical Society · 2024Article
- Dual reactivity disulfide bridging reagents; enabling new approaches to antibody fragment bioconjugation.Chemical science · 2022Article
- Enabling the next steps in cancer immunotherapy: from antibody-based bispecifics to multispecifics, with an evolving role for bioconjugation chemistry.RSC chemical biology · 2022Review
- An overview of chemo- and site-selectivity aspects in the chemical conjugation of proteins.Royal Society open science · 2022Article
- Site-selective lysine conjugation methods and applications towards antibody-drug conjugates.Chemical communications (Cambridge, England) · 2021Review
- DNAzymes for amine and peptide lysine acylation.Organic & biomolecular chemistry · 2021Article
- Pyrocinchonimides Conjugate to Amine Groups on Proteins via Imide Transfer.Bioconjugate chemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The modification of lysine residues with acylating agents has represented a ubiquitous approach to the construction of antibody conjugates, with the resulting amide bonds being robustly stable and clinically validated. However, the conjugates are highly heterogeneous, due to the presence of numerous lysines on the surface of the protein, and greater control of the sites of conjugation are keenly sought. Here we present a novel approach to achieve the targeted modification of lysines distal to an antibody fragment's binding site, using a disulfide bond as a temporary 'hook' to deliver the acylating agent. This cysteine-to-lysine transfer (CLT) methodology offers greatly improved homogeneity of lysine conjugates, whilst retaining the advantages offered by the formation of amide linkages.
Identifiers
What OpenQuestion holds
Registered trials
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.