Expanding the payload scope in antibody-drug conjugates by delivery of hydroxy-containing drugs through self-immolative phosphoramidates

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Authors: Philipp Ochtrop, Anil P. Jagtap, Jan G. Felber, Simon Vogt, Sarah Herterich, Isabelle Mai, Philipp Cyprys, Saskia Schmitt, Sarah Payer, Annabel Kitowski, Swetlana Wunder, Paul Machui
+9 more Julia Ines Brandmeier, Natascia Leonardi, Elizaveta Poliak, Christian P. R. Hackenberger, Olivier Marcq, Dominik Schumacher, Jonas Helma, Annette M. Vogl, Marc‐André Kasper
Cited by: 5
References: 77

Abstract

Despite recent advances in targeted drug delivery, approved Antibody-Drug-Conjugates (ADCs) are still limited by the delivery of a restricted set of payloads with limited modes of action (MOA). Versatile linkers, applicable to functional groups prevalent across diverse pharmacophores are needed to expand this space. We present phosphoramidate-based self-immolative linker-units that facilitate stable attachment in serum and traceless drug release in the target cell of aliphatic and aromatic alcohols. Studies with camptothecins show that stability and release are tunable and that various intracellular trigger events can be exploited to ensure traceless drug delivery. Superior stability, in vivo efficacy, and pharmacokinetics (PK) compared to approved camptothecin ADCs are demonstrated. Moreover, we report targeted delivery of 10 different hydroxy-containing cytotoxins with different intracellular MOAs. In vivo studies with gemcitabine show excellent PK and efficacy, unlocking gemcitabine’s full potential and illustrating the ability of the phosphoramidate-based linker system to expand the payload space for ADCs. Approved antibody–drug conjugates (ADCs) remain constrained by a limited repertoire of payloads with restricted modes of action. Here, the authors present phosphoramidate-based self-immolative linker units that facilitate stable attachment in serum and traceless drug release in the target cell from aliphatic and aromatic alcohols with various modes of action.

Fields of Study & Subjects

HER2/EGFR in Cancer Research Monoclonal and Polyclonal Antibodies Research Click Chemistry and Applications

Publication details

Journal / source
Nature Communications
Publisher
Springer Science and Business Media LLC
Volume
17
Issue
1
Pages
759–759
Publication date
20 January 2026
Language
EN