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Area of Science:

  • Biopharmaceutical development
  • Protein aggregation
  • Interface science

Background:

  • Protein aggregation is a critical quality issue in biopharmaceutical development.
  • Protein-interface interactions often trigger aggregation in aqueous solutions.
  • Existing high-throughput assays for interface-induced protein instability are limited.

Purpose of the Study:

  • To develop a controlled, high-throughput assay for protein instability at interfaces.
  • To mimic air-water interfaces using a novel nanoparticle-based method.
  • To screen and optimize conditions preventing surface-induced protein aggregation.

Main Methods:

  • Development of a surface-mediated stress assay using polymeric nanoparticles.
  • Implementation on a high-throughput microfluidic platform with picoliter droplets.
  • Evaluation of protein instability at hydrophobic interfaces under controlled conditions.

Main Results:

  • Hydrophobic nanoparticles effectively destabilize large proteins like antibodies.
  • The assay evaluates protein instability at hydrophobic interfaces within minutes.
  • The method successfully identified optimal Tween 80 concentrations to prevent antibody instability.

Conclusions:

  • The hydrophobic nanoparticle surface-mediated stress assay (HNSSA) is a powerful tool for assessing protein instability.
  • HNSSA mimics air-water interfaces and aids in optimizing buffer composition.
  • This assay facilitates early-stage selection of stable biotherapeutic candidate molecules.