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Cysteine-To-Lysine Transfer Antibody Fragment Conjugation

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.

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Publication details

The article was received on 01 Aug 2019, accepted on 11 Oct 2019 and first published on 11 Oct 2019


Article type: Edge Article
DOI: 10.1039/C9SC03825F
Chem. Sci., 2019, Accepted Manuscript
  • Open access: Creative Commons BY license
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    Cysteine-To-Lysine Transfer Antibody Fragment Conjugation

    N. Forte, I. Benni, K. Karu, V. Chudasama and J. Baker, Chem. Sci., 2019, Accepted Manuscript , DOI: 10.1039/C9SC03825F

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