Toward homogenous antibody drug conjugates using enzyme-based conjugation approaches

Ahmad Fawzi Hussain*, Armin Grimm, Wenjie Sheng, Chaoyu Zhang, Marwah Al-Rawe, Karen Bräutigam, Mobarak Abu Mraheil, Felix Zeppernick, Ivo Meinhold-Heerlein

*Corresponding author for this work

Abstract

In the last few decades, antibody-based diagnostic and therapeutic applications have been well established in medicine and have revolutionized cancer managements by improving tumor detection and treatment. Antibodies are unique medical elements due to their powerful properties of being able to recognize specific antigens and their therapeutic mechanisms such as blocking specific pathways, antibody-dependent cellular cytotoxicity, and complement-dependent cytotoxicity. Furthermore, modification techniques have paved the way for improving antibody properties and to develop new classes of antibody-conjugate-based diagnostic and therapeutic agents. These techniques allow arming antibodies with various effector molecules. However, these techniques are utilizing the most frequently used amino acid residues for bioconjugation, such as cysteine and lysine. These bioconjugation approaches generate heterogeneous products with different functional and safety profiles. This is mainly due to the abundance of lysine and cysteine side chains. To overcome these limitations, different site-direct conjugation methods have been applied to arm the antibodies with therapeutic or diagnostics molecules to generate unified antibody conjugates with tailored properties. This review summarizes some of the enzyme-based site-specific conjugation approaches.

Original languageEnglish
Article number343
JournalPharmaceuticals
Volume14
Issue number4
DOIs
Publication statusPublished - 08.04.2021

Research Areas and Centers

  • Research Area: Luebeck Integrated Oncology Network (LION)
  • Centers: University Cancer Center Schleswig-Holstein (UCCSH)

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