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Process and Formulation Effects on Protein Structure in Lyophilized Solids Using Mass Spectrometric Methods.

Lavanya K Iyer1, Gregory A Sacha2, Balakrishnan S Moorthy1

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Controlled ice nucleation and sucrose improve lyophilized myoglobin structure and cake uniformity. These techniques enhance protein stability during freeze-drying, crucial for biopharmaceutical development.

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Area of Science:

  • Biochemistry
  • Pharmaceutical Sciences
  • Materials Science

Background:

  • Lyophilization (freeze-drying) is critical for stabilizing proteins like myoglobin.
  • Understanding formulation and process impacts on protein structure is essential for drug development.

Purpose of the Study:

  • To investigate the effects of controlled ice nucleation and sucrose on myoglobin (Mb) structure and cake morphology during pilot-scale lyophilization.
  • To evaluate the utility of advanced analytical techniques for characterizing freeze-dried protein formulations.

Main Methods:

  • Lyophilization of myoglobin with and without sucrose, with and without controlled ice nucleation.
  • Characterization of cake morphology using scanning electron microscopy.
  • Monitoring protein structural changes using solid-state Fourier-transform infrared spectroscopy, hydrogen-deuterium exchange-mass spectrometry, and photolytic labeling-mass spectrometry (ssPL-MS).

Main Results:

  • Controlled nucleation yielded uniform cake structures and consistent nucleation temperatures (∼-5°C).
  • Sucrose-containing formulations (Mb-B) exhibited superior protein structure retention compared to those without sucrose (Mb-A).
  • ssPL-MS indicated increased protein modification in Mb-B lyophilized with controlled nucleation, suggesting enhanced structural integrity.

Conclusions:

  • Controlled ice nucleation and sucrose are beneficial for improving lyophilized myoglobin cake structure and protein stability.
  • Solid-state hydrogen-deuterium exchange-mass spectrometry and ssPL-MS are valuable tools for assessing formulation- and process-induced changes in lyophilized proteins.
  • Optimizing lyophilization parameters can significantly enhance the quality and stability of protein-based therapeutics.