Developing safer, more effective antibody–drug conjugates (ADCs) requires precise control over how cytotoxic payloads are attached to monoclonal antibodies. Traditional lysine‑ or cysteine‑based conjugation methods often lead to heterogeneous products with variable drug‑to‑antibody ratios, which can impact stability, consistency, and overall therapeutic performance.
This whitepaper explores a chemoenzymatic conjugation approach that enables highly controlled, site‑specific payload attachment to the native N‑glycan of antibodies. By combining enzymatic glycan remodeling with copper‑free click chemistry, the method delivers homogeneous, stable ADCs without requiring antibody engineering.
Supported by comparative in vitro and in vivo studies, this approach demonstrates strong potential to improve therapeutic index through enhanced stability, predictable conjugation, and efficient payload delivery.
Download the whitepaper to learn more.
