Tag‐Free Enzymatic Modification for Antibody−Drug Conjugate Production
Authors:
- 20 December 2022
- journal article
- review article
- Published by Wiley in ChemistrySelect
- Vol. 7 (48)
Abstract
Currently, although >10 antibody−drug conjugates (ADCs) are available in the market, most of them (10 ADCs) have broad drug distribution, thereby potentially limiting their therapeutic index. The ADC industry is shifting from random conjugation technology to site‐specific conjugation technology to overcome this issue. Enzymatic site‐specific conjugation is a promising cutting‐edge technology owing to its mild conjugation conditions. This review discussed enzymatic conjugation strategies for producing ADCs via modifying native antibodies without using a tag moiety. We described the comparison of the three main conjugation technologies used to produce site‐specific ADCs. Each of the three enzymatic approaches described in this review differs in their advantages and disadvantages, providing pharmaceutical companies the option to select an approach suitable to their purpose and/or target protein.Keywords
This publication has 95 references indexed in Scilit:
- Marketed therapeutic antibodies compendiummAbs, 2012
- Site‐Specific and Stoichiometric Modification of Antibodies by Bacterial TransglutaminaseAngewandte Chemie International Edition, 2010
- Yeast Display Evolution of a Kinetically Efficient 13-Amino Acid Substrate for Lipoic Acid LigaseJournal of the American Chemical Society, 2009
- The economies of synthesisChemical Society Reviews, 2009
- Sortase‐Mediated Ligation: A Gift from Gram‐Positive Bacteria to Protein EngineeringChemBioChem, 2009
- Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic indexNature Biotechnology, 2008
- An Eight Residue Fragment of an Acyl Carrier Protein Suffices for Post-Translational Introduction of Fluorescent Pantetheinyl Arms in Protein Modification in vitro and in vivoJournal of the American Chemical Society, 2008
- Metabolic biotinylation of recombinant antibody by biotin ligase retained in the endoplasmic reticulumBiomolecular Engineering, 2007
- Structure-based Design of β1,4-Galactosyltransferase I (β4Gal-T1) with Equally Efficient N-Acetylgalactosaminyltransferase ActivityJournal of Biological Chemistry, 2002
- A minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylationProtein Science, 1999