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Exploring a role for flow-induced aggregation assays in platform formulation optimisation for antibody-based

Leon F Willis1, Vishal Toprani2, Sashini Wijetunge2

  • 1Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds UK LS2 9JT.

Journal of Pharmaceutical Sciences
|November 4, 2024
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Summary

The Extensional Flow Device (EFD) quickly identifies stable therapeutic monoclonal antibodies and Fc-fusion proteins. This method aids in selecting optimal formulations for next-generation biologics, reducing development time and material use.

Keywords:
aggregationantibodydevelopability screeningphysicochemical propertiesprotein aggregationprotein formulation

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Area of Science:

  • Biopharmaceutical development
  • Protein aggregation studies
  • Formulation science

Background:

  • Therapeutic monoclonal antibody (mAb) development time is reduced by formulation platforms and developability assays.
  • Protein stability assessment under various stresses, including hydrodynamic forces, is crucial.
  • A low-volume Extensional Flow Device (EFD) was previously developed to identify robust protein sequences.

Purpose of the Study:

  • To study the aggregation of mAbs and Fc-fusion proteins using the EFD and orbital shaking under different formulations.
  • To investigate the relationship between EFD, orbital shaking, and formulation optimization.
  • To evaluate the potential of the EFD in formulation optimization for biologics.

Main Methods:

  • Utilized a low-volume Extensional Flow Device (EFD) to apply defined fluid flow fields to proteins.
  • Compared EFD with orbital shaking assays under various formulation conditions.
  • Investigated aggregation of monoclonal antibodies (mAbs) and Fc-fusion proteins.

Main Results:

  • EFD identified the least aggregation-prone molecules faster and with less material than traditional methods.
  • EFD differentiated between various formulations, showing polysorbate 80 stabilized Fc-fusion proteins against aggregation.
  • Identified common formulation additives affecting aggregation under EFD stress and factors modulating aggregation mechanisms.

Conclusions:

  • The EFD is an efficient tool for early-stage screening of protein developability and formulation optimization.
  • EFD data can guide the selection of platform formulations for next-generation therapeutics, including fusion proteins.
  • Understanding formulation effects on aggregation mechanisms aids in developing more stable biologic drugs.