Predicting Agitation Stability of Monoclonal Antibodies during Developability Assessment
), hydrophobic interaction chromatography retention time, and relative monomer yield after isothermal refolding from chemical denaturants. Notably, none of these parameters correlated with agitation-induced aggregation. Finally, we assessed the surface properties of the mAbs via drop shape analysis and found that the combination of surface pressure and elastic modulus yields a good correlation with the concentration of micrometre-sized aggregates formed due to agitation. Overall, these findings highlight limitations in predicting mAb interfacial stability using standard developability assays and underscore the importance of studying antibody behavior at interfaces.
Authors
- Zahari Vinarov (ORCID: https://orcid.org/0000-0003-1857-1840)
- Utku Özbulak (ORCID: https://orcid.org/0000-0003-3084-6034)
- Kevin Braeckmans (ORCID: https://orcid.org/0000-0002-7993-6295)
- Wesley De Neve (ORCID: https://orcid.org/0000-0002-8190-3839)
- Hristo L. Svilenov (ORCID: https://orcid.org/0000-0001-5863-9569)
- Nevena Pagureva
- Slavka Tcholakova (ORCID: https://orcid.org/0000-0001-8091-7529)
- Michaela Cohrs (ORCID: https://orcid.org/0000-0003-1195-534X)
- Stefaan De Smedt
Institutions
- HOGENT University of Applied Sciences and Arts (BE)
- Ghent University (BE)
- Ghent University Global Campus (KR)
- Sofia University "St. Kliment Ohridski" (BG)
- Technical University of Munich (DE)
Publication Details
- Journal
- Molecular Pharmaceutics
- Published
- 2026-04-24
- DOI
- https://doi.org/10.1021/acs.molpharmaceut.6c00092
- Primary Topic
- Protein purification and stability
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Fonds Wetenschappelijk Onderzoek
- NextGenerationEU