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Correlation between the Protein Pharmaceutical Surface Activity and Interfacial Stability.

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Protein drug stability is crucial for formulations. This study reveals that protein surface activity significantly impacts interfacial stability, challenging the sole reliance on surfactants for formulation development.

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Area of Science:

  • Pharmaceutical Sciences
  • Biochemistry
  • Physical Chemistry

Background:

  • Protein drug stability in aqueous formulations is critical, especially concerning air-liquid interface interactions.
  • Nonionic surfactants are commonly used to mitigate protein adsorption and instability at interfaces.
  • Previous research has overlooked the intrinsic surface properties of protein drugs themselves.

Purpose of the Study:

  • To investigate the correlation between protein drugs' surface behavior and their interfacial stability.
  • To understand the competitive adsorption dynamics between proteins and surfactants at the air-liquid interface.
  • To highlight the importance of protein intrinsic properties in formulation development.

Main Methods:

  • Utilized a force tensiometer to measure surface tension reduction.
  • Tracked the competition between protein drugs and surfactants at the air-liquid interface.
  • Evaluated surface behavior of various protein types (monoclonal antibodies, bispecific monoclonal antibodies, antibody-drug conjugates) under different storage temperatures.

Main Results:

  • Protein surface activity varies with storage temperature and protein type.
  • At 5 °C, protein surface activity was observed to be greater than that of surfactants.
  • Demonstrated that proteins' interfacial adsorption capacity is a significant factor in formulation stability, comparable to surfactants.

Conclusions:

  • The intrinsic surface activity of protein drugs is a critical, often neglected, factor in achieving interfacial stability in formulations.
  • Formulation strategies should consider the inherent surface properties of protein drugs alongside surfactant use.
  • These findings offer new perspectives for preformulation studies and the development of stable therapeutic protein formulations.