Understanding Antibody Stability in Biotherapeutics
Author Information
Author(s): Christofi Emilia, O’Hanlon Mark, Curtis Robin, Barman Arghya, Keen Jeff, Nagy Tibor, Barran Perdita
Primary Institution: Manchester Institute of Biotechnology, University of Manchester
Hypothesis
How do solution condition changes impact the structural integrity of a biopharmaceutical across the processing pipeline?
Conclusion
The study found that mAb4 exhibits increased structural stability in higher ionic strength environments, while also revealing distinct unfolding patterns compared to Herceptin.
Supporting Evidence
- mAb4 shows distinct unfolding patterns in activated ion mobility mass spectrometry compared to Herceptin.
- Hydrogen-deuterium exchange mass spectrometry revealed substantial structural changes in mAb4 during purification.
- mAb4's structural stability improves in high-salt environments.
Takeaway
This study looks at how different conditions during the production of antibodies can change their structure and stability, which is important for making effective medicines.
Methodology
The study used hybrid mass spectrometry techniques, including activated ion mobility mass spectrometry (aIM-MS) and hydrogen-deuterium exchange mass spectrometry (HDX-MS), to assess the structural stability of a model monoclonal antibody (mAb4) during downstream processing.
Limitations
The study primarily focuses on a single model antibody and may not generalize to all monoclonal antibodies.
Digital Object Identifier (DOI)
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