Forte, N;
Benni, I;
Karu, K;
Chudasama, V;
Baker, JR;
(2019)
Cysteine-to-lysine transfer antibody fragment conjugation.
Chemical Science
, 10
(47)
pp. 10919-10924.
10.1039/c9sc03825f.
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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.
| Type: | Article |
|---|---|
| Title: | Cysteine-to-lysine transfer antibody fragment conjugation |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1039/c9sc03825f |
| Publisher version: | https://doi.org/10.1039/c9sc03825f |
| Language: | English |
| Additional information: | This article is licensed under a Creative Commons Attribution 3.0 Unported Licence https://creativecommons.org/licenses/by/3.0/ |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > UCL BEAMS UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Chemistry |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10084330 |
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