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In Situ Characterization of the Microstructural Evolution of Biopharmaceutical Solid-State Formulations with Implications for Protein Stability
- Source :
- Molecular Pharmaceutics; 20240101, Issue: Preprints
- Publication Year :
- 2024
-
Abstract
- Lyophilized and spray-dried biopharmaceutical formulations are used to provide long-term stability for storage and transport, but questions remain about the molecular structure in these solid formulations and how this structure may be responsible for protein stability. Small-angle neutron scattering with a humidity control environment is used to characterize protein-scale microstructural changes in such solid-state formulations as they are humidified and dried in situ. The findings indicate that irreversible protein aggregates of stressed formulations do not form within the solid-state but do emerge upon reconstitution of the formulation. After plasticization of the solid-state matrix by exposure to humidity, the formation of reversibly self-associating aggregates can be detected in situ. The characterization of the protein-scale microstructure in these solid-state formulations facilitates further efforts to understand the underlying mechanisms that promote long-term protein stability.
Details
- Language :
- English
- ISSN :
- 15438384 and 15438392
- Issue :
- Preprints
- Database :
- Supplemental Index
- Journal :
- Molecular Pharmaceutics
- Publication Type :
- Periodical
- Accession number :
- ejs47214802
- Full Text :
- https://doi.org/10.1021/acs.molpharmaceut.8b00935