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Colloidal precipitates01:09

Colloidal precipitates

477
The high insolubility of some precipitates can result in an unfavorable relative supersaturation. This can lead to colloidal particles with a large surface-to-mass ratio, where adsorption is promoted. For instance, in the precipitation of silver chloride, silver ions are adsorbed on the surface of the colloidal particles, forming a primary layer. This layer attracts ions of opposite charge (such as nitrate ions), forming a diffuse secondary layer of adsorbed ions. This electric double layer...
477

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The value of spray drying as stabilization process for proteins.

Katharina Tatjana Kopp1, Maarten De Beer2, Jody Voorspoels2

  • 1Eurofins Amatsigroup, Industriepark-Zwijnaarde 7B, 9052 Gent, Belgium; Drug Delivery and Disposition, KU Leuven, Department of Pharmaceutical and Pharmacological Sciences, Campus Gasthuisberg ON2, Herestraat 49, 3000 Leuven, Belgium.

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Summary

Formulation strategies using buffers and excipients can enhance protein stability during spray drying (SD). This study explored predicting solid-state protein stability from solution-state data, finding BSA and lysozyme highly stable post-SD, while IgG showed significant concentration loss.

Keywords:
Differential Scanning Fluorimetry/Static Light ScatteringExcipientsProtein stabilityProteinsSolidificationSpray drying

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Area of Science:

  • Pharmaceutical Sciences
  • Biotechnology
  • Materials Science

Background:

  • Protein instability in solution necessitates stabilization methods for therapeutic applications.
  • Solidification techniques like spray drying (SD) can improve protein stability but involve process-related stresses.
  • Formulation development with buffers and excipients is crucial to mitigate stress during protein solidification.

Purpose of the Study:

  • To identify optimal buffers and excipients for stabilizing model proteins (BSA, IgG, lysozyme) in solution.
  • To investigate the correlation between solution-state protein stability and solid-state stability after spray drying (SD).
  • To assess the feasibility of predicting solid-state protein behavior using solution-state screening data.

Main Methods:

  • Differential scanning fluorimetry (DSF) and static light scattering (SLS) for solution-state screening.
  • Design of experiments (DoE) approach to optimize buffer and excipient formulations.
  • Spray drying (SD) of protein formulations.
  • Analytical characterization post-SD including chromatography (RPC, SEC), dynamic light scattering (DLS), UV-Vis, and circular dichroism (CD).

Main Results:

  • BSA and lysozyme demonstrated high stability and minimal changes after SD.
  • IgG exhibited greater sensitivity to the solidification process, with over 15% loss in initial protein concentration.
  • The study compared stability data from solution state (DSF/SLS) with post-SD analytical results.

Conclusions:

  • Specific buffers and excipients can effectively stabilize model proteins during spray drying (SD).
  • While BSA and lysozyme were robust, IgG stability requires further optimization for SD.
  • Predicting solid-state protein stability from solution-state data warrants further investigation, potentially with non-reconstitution-based analytical methods.