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Container surfaces significantly impact therapeutic antibody aggregation, affecting product quality. Elevated temperatures cause particle adhesion, masking aggregation, while long-term storage reveals true particle increases, necessitating careful analysis.

Keywords:
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Area of Science:

  • Biopharmaceutical development
  • Protein aggregation science

Background:

  • Predicting antibody aggregation is crucial for therapeutic quality and safety.
  • Container surfaces can influence protein aggregation kinetics.

Purpose of the Study:

  • To investigate the role of container surfaces on monoclonal antibody (mAb) aggregation.
  • To assess aggregation under elevated temperature and long-term storage conditions without mechanical stress.

Main Methods:

  • Systematic study of aggregation across different proteins, vial materials, and storage temperatures.
  • Utilized size exclusion chromatography and micro-flow imaging for aggregate quantification.
  • Employed optical and atomic force microscopy to analyze vial surface interactions.

Main Results:

  • Protein particles adhere to vial surfaces at elevated temperatures, leading to underestimated aggregation.
  • At 5°C, particles do not adhere, increasing bulk concentration unpredictably by standard methods.
  • Identified specific protein-surface interactions driving nanoscale oligomer formation.

Conclusions:

  • Interpretations of stability data require careful consideration of temperature and vial type.
  • A combined approach analyzing vial surfaces and bulk solution is proposed for comprehensive understanding of protein aggregation.