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This Expert Insights eBook gives scientists and development teams a chemistry-to-characterization view of antibody-drug conjugates (ADCs), from bioconjugation and linker design through the LC–MS methods used to quantify each ADC species.
What you will learn about:
- How click-type and site-selective bioconjugation reactions modify antibodies at lysine, cysteine, and tyrosine residues
- Why linker chemistry and conjugation strategy now drive an ADC’s therapeutic index, homogeneity, and DAR control
- What discontinued ADCs reveal about linker stability, payload selection, and off-target toxicity
- How advanced cleavable linkers and hydrophilic spacers improve plasma stability and payload release
- Which LC–MS strategies quantify intact ADC, total antibody, payload, and catabolite species, and where current methods fall short
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More Information
Antibody-drug conjugates hold a central place in targeted cancer therapy, but their performance rests on more than antigen recognition. Payload conjugation strategy, linker stability in circulation, drug release efficiency, and drug-to-antibody ratio (DAR) all shape efficacy and toxicity. This eBook brings together three complementary perspectives on ADC chemistry: the bioconjugation reactions behind modern protein modification, innovation in linker and site-specific conjugation, and the LC–MS methods that characterize each molecular species during development.
Articles contained in the collection:
- Stump B. Click-bioconjugation: modifying proteins using click-like chemistry. ChemBioChem. 2022;23(16):e202200016. doi:10.1002/cbic.202200016
- Matsuda Y, et al. Advanced antibody-drug conjugates design: innovation in linker chemistry and site-specific conjugation technologies. ChemBioChem. 2025. doi:10.1002/cbic.202500305
- Buitelaar PLM, et al. An overview of liquid chromatography-mass spectrometry (LC–MS) methods for the quantification of antibody-drug conjugates. Biomed Chromatogr. 2026. doi:10.1002/bmc.70334
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