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Updated: Jan 21, 2026

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction
Published on: September 14, 2018
Alteration of Physicochemical Properties for Antibody-Drug Conjugates and Their Impact on Stability
Jakob W Buecheler1, Matthias Winzer2, Christian Weber2
1Division of Pharmaceutics, Friedrich-Alexander University (FAU) Erlangen-Nuernberg, Freeze Drying Focus Group, 91058 Erlangen, Germany; Merck Healthcare KGaA, Discovery and Development Technologies, 64293 Darmstadt, Germany.
Abstract:
Antibody conjugates, in particular antibody-drug conjugates (ADCs), are a fast-growing area in research and in the pharmaceutical industry. The covalent attachment of an antibody to a chemical moiety can be an effective measure for drug targeting or can also positively impact pharmacokinetics of small molecular compounds by serum half-life extension. Stability, physicochemical properties, and degradation pathways of biotherapeutics or small molecule therapeutics are often not totally known and understood. However, ADCs represent a hybrid of small molecular and macromolecular components, and their properties are still not fully understood and described. This review discusses the alteration of the physicochemical properties of antibodies upon conjugation of chemical moieties to its surface and the resulting impact on ADC stability.
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