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Tungsten-induced protein aggregation: solution behavior.

Yijia Jiang1, Yasser Nashed-Samuel, Cynthia Li

  • 1Formulation and Analytical Resources, Amgen, Inc., One Amgen Center Drive, Thousand Oaks, California 91320, USA. yjiang@amgen.com

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Tungsten from prefilled syringes (PFSs) can cause protein aggregation. Tungsten pin extract was more effective than commercial sources, with aggregation influenced by pH, tungsten species, and concentration.

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Area of Science:

  • Biopharmaceutical manufacturing
  • Materials science
  • Protein chemistry

Background:

  • Tungsten is used in prefilled syringes (PFSs).
  • Tungsten has been linked to protein aggregation in PFSs.
  • The exact mechanism and influencing factors require further investigation.

Purpose of the Study:

  • To investigate the relationship between tungsten, PFSs, and protein aggregation.
  • To compare the protein aggregation potential of tungsten from PFS pins versus commercial sources.
  • To identify factors influencing tungsten-induced protein aggregation.

Main Methods:

  • Spiking model protein solutions with tungsten species from PFS pins and commercial sources.
  • Comparing visible and soluble protein aggregate formation.
  • Analyzing the effect of pH, tungsten species, and concentration on aggregation.
  • Characterizing the structure and reversibility of tungsten-induced aggregates.

Main Results:

  • Tungsten from both sources induced visible protein particles and aggregates.
  • Tungsten extracted from PFS pins was more potent in inducing soluble protein aggregates.
  • Protein aggregation was dependent on pH, tungsten species, and concentration, with lower pH and higher concentration increasing aggregation.
  • Tungsten-induced aggregates exhibited mostly native-like structure and were partly reversible.
  • Aggregation mechanism appears to involve electrostatic interactions between tungsten and protein molecules.
  • Required tungsten levels exceeded typical soluble tungsten levels in commercial PFSs.

Conclusions:

  • Tungsten, particularly from PFS pins, is a significant factor in protein aggregation.
  • Protein aggregation induced by tungsten is controllable by factors like pH and concentration.
  • The findings are crucial for understanding and mitigating protein aggregation in PFS formulations.
  • Further research into tungsten-protein interactions is warranted for biopharmaceutical development.