Abstract
Purpose
This study aimed to investigate the effects of preparation conditions and external factors, particularly ultraviolet (UV) exposure, on inline-filter clogging in liquid monoclonal antibody (l-mAb) formulations. Bevacizumab (BmAb) was used as a model drug to address the critical question of how UV exposure impacts protein stability and filter performance during clinical administration.
Methods
Bevacizumab solutions were exposed to UV-C (254 nm) light to evaluate its effects on protein stability and filter clogging. Scanning electron microscopy (SEM) was used to visualize protein aggregates on the filter surface. Dynamic light scattering (DLS) analysis measured particle size distribution and average particle size. To assess the effectiveness of light shielding, additional samples were prepared under conditions that minimized UV exposure.
Results
UV-C exposure induced significant precipitate formation, with SEM images revealing protein aggregates on the filter surface. DLS analysis showed a broader particle size distribution and an increase in average particle size (18.1 nm) in UV-exposed solutions compared to non-exposed controls. Light shielding effectively suppresses precipitate formation, maintaining the stability of BmAb solutions and preventing inline-filter clogging.
Conclusion
UV-C destabilizes BmAb solutions, leading to protein aggregation and inline-filter clogging. Light shielding was identified as an effective strategy to maintain the stability and safety of l-mAb formulations, particularly in settings where prolonged exposure to environmental light is possible. These findings emphasize the importance of implementing protective measures against UV exposure and call for further research on additional environmental factors and optimized protocols to enhance l-mAb formulation reliability.
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