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Issue 47, 2019
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Cysteine-to-lysine transfer antibody fragment conjugation

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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.

Graphical abstract: Cysteine-to-lysine transfer antibody fragment conjugation

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Supplementary files

Article information


Submitted
01 Aug 2019
Accepted
11 Oct 2019
First published
11 Oct 2019

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2019,10, 10919-10924
Article type
Edge Article

Cysteine-to-lysine transfer antibody fragment conjugation

N. Forte, I. Benni, K. Karu, V. Chudasama and J. R. Baker, Chem. Sci., 2019, 10, 10919
DOI: 10.1039/C9SC03825F

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