A comparative study of the developability of full-length antibodies, fragments, and bispecific formats reveals higher stability risks for engineered constructs

• Published in: mAbs Vol. 16; no. 1; p. 2403156
• Main Authors: Condado-Morales, Itzel, Dingfelder, Fabian, Waibel, Isabel, Turnbull, Oliver M, Patel, Bhargav, Cao, Zheng, Rose Bjelke, Jais, Nedergaard Grell, Susanne, Bennet, Anja, Hummer, Alissa M, Raybould, Matthew I J, Deane, Charlotte M, Egebjerg, Thomas, Lorenzen, Nikolai, Arosio, Paolo
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 31.12.2024; Taylor & Francis Group
• Subjects: aggregation; Antibodies, Bispecific - chemistry; Antibodies, Bispecific - genetics; Antibodies, Bispecific - immunology; Antibodies, Monoclonal - chemistry; Antibodies, Monoclonal - genetics; Antibodies, Monoclonal - immunology; Antibody; bispecifics; developability; Fragmentation; fragments; Humans; Protein Engineering - methods; Protein Stability; Single-Chain Antibodies - chemistry; Single-Chain Antibodies - genetics; Single-Chain Antibodies - immunology; Tumor Necrosis Factor-alpha - immunology; antibody formats; developability; Self-association; Antibody; Shelf-life stability; aggregation; Biophysics; Fragmentation; bispecifics; Colloidal stability; scFv; Formulation; fragments

Engineered antibody formats, such as antibody fragments and bispecifics, have the potential to offer improved therapeutic efficacy compared to traditional full-length monoclonal antibodies (mAbs). However, the translation of these non-natural molecules into successful therapeutics can be hampered by...