In vitro stress testing demonstrates robust structural stability and maintained binding in bispecific antibodies, highlighting the therapeutic viability of the B-Body platform.
The B-Body® Platform was utilized to generate a bispecific antibody (bsAb) containing two distinct fragment antigen-binding (Fab) regions, enabling dual epitope targeting. This platform employs knob-into-hole technology, a domain swap strategy, along with proprietary symmetrical heavy and light chain inversions in the Fab arms, resulting in high transfection expression levels, excellent solubility, and low viscosity. To assess stability, degradation pathways, and functionality, a forced degradation study was conducted on the bsAb under various stress conditions, including heat, accelerated stability, pH, oxidation, and forced glycation. Analytical and biological characterization assays, including size-exclusion chromatography, ion-exchange chromatography, capillary electrophoresis-sodium dodecyl sulfate, LC-MS/MS peptide mapping, and enzyme-linked immunosorbent assay (ELISA) were used to evaluate the effects of these stress conditions. The study revealed modest size variants and post-translational modifications, including deamidation, succinimides, and oxidation et al. while maintaining consistent biological functionality. These findings highlight the favorable stability of the bsAb generated using the B-Body Platform, demonstrating its potential as a platform for the development of novel therapeutic bispecific antibodies.
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Chen et al. (2026) studied this question.
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