@article{discovery10135863,
           month = {September},
            year = {2021},
           title = {Site-selective lysine conjugation methods and applications towards antibody-drug conjugates},
         journal = {Chemical Communications},
            note = {This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.},
          author = {Haque, M and Forte, N and Baker, JR},
        abstract = {Site-selective protein modification is of significant interest in chemical biology research, with lysine residues representing a particularly challenging target. Whilst lysines are popular for bioconjugation, due to their nucleophilicity, solvent accessibility and the stability of the resultant conjugates, their high abundance means site-selectivity is very difficult to achieve. Antibody-drug conjugates (ADCs) present a powerful therapeutic application of protein modification, and have often relied extensively upon lysine bioconjugation for their synthesis. Here we discuss advances in methodologies for achieving site-selective lysine modification, particularly within the context of antibody conjugate construction, including the cysteine-to-lysine transfer (CLT) protocol which we have recently reported.},
             url = {https://doi.org/10.1039/D1CC03976H}
}