期刊
CHEMICAL COMMUNICATIONS
卷 57, 期 82, 页码 10689-10702出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc03976h
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资金
- MRC UCL DTP [MR/N013867/1]
- EPSRC [EP/R034621/1]
- EPSRC [EP/R034621/1] Funding Source: UKRI
Selective modification of lysine residues presents a significant challenge due to their popularity in bioconjugation. Antibody-drug conjugates heavily rely on lysine bioconjugation for synthesis, highlighting the importance of achieving site-selective lysine modification methodologies.
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.
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