Unknown

Dataset Information

0

Site-selective lysine conjugation methods and applications towards antibody-drug conjugates.


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.

SUBMITTER: Haque M 

PROVIDER: S-EPMC8516052 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Site-selective lysine conjugation methods and applications towards antibody-drug conjugates.

Haque Muhammed M   Forte Nafsika N   Baker James R JR  

Chemical communications (Cambridge, England) 20211014 82


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 rel  ...[more]

Similar Datasets

| S-EPMC10522789 | biostudies-literature
| S-EPMC11417993 | biostudies-literature
| S-EPMC7555909 | biostudies-literature
| S-EPMC6698857 | biostudies-literature
| S-EPMC4260860 | biostudies-literature
| S-EPMC8048973 | biostudies-literature
| S-EPMC8081041 | biostudies-literature
| S-EPMC7518637 | biostudies-literature
| S-EPMC8549674 | biostudies-literature
2023-02-14 | PXD040111 |