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Related Experiment Videos

Self-buffering antibody formulations.

Yatin R Gokarn1, Eva Kras, Carrie Nodgaard

  • 1Department of Pharmaceutics, Amgen Inc., Thousand Oaks, California 91320, USA. ygokarn@amgen.com

Journal of Pharmaceutical Sciences
|November 21, 2007
PubMed
Summary
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High-concentration monoclonal antibody formulations can utilize the antibody's inherent "self-buffering" capacity. This novel approach enhances stability and offers a promising alternative for protein-based drug development.

Area of Science:

  • Biopharmaceutical development
  • Protein formulation science
  • Antibody engineering

Background:

  • Monoclonal antibodies (mAbs) often necessitate high-concentration formulations for therapeutic efficacy.
  • Achieving stable formulations around pH 5.0 presents formulation challenges.
  • Conventional buffering agents can sometimes promote unwanted protein aggregation.

Purpose of the Study:

  • To investigate the self-buffering capabilities of monoclonal antibodies (mAbs) in the pH 4-6 range.
  • To evaluate the stability of self-buffered mAb formulations compared to conventionally buffered ones.
  • To explore the potential of self-buffering as a strategy for high-concentration protein formulations.

Main Methods:

  • Measured buffer capacities of four IgG2 molecules (mAb1-mAb4) between pH 4-6.

Related Experiment Videos

  • Conducted accelerated stability studies at 50°C for 3 weeks comparing self-buffered and conventionally buffered mAb1 formulations.
  • Performed long-term stability studies at 37°C and 4°C for 12 months.
  • Assessed stability through freeze-thaw cycling (-20°C to room temperature).

    • Main Results:

    • mAb buffer capacity increased linearly with concentration, surpassing 10 mM acetate at 60-80 mg/mL.
    • Self-buffered mAb1 formulations exhibited superior resistance to soluble aggregate formation compared to conventional buffers (acetate, glutamate, succinate).
    • Long-term and freeze-thaw stability of self-buffered mAb1 formulations were comparable to conventionally buffered counterparts, with no significant pH change over 12 months.

    Conclusions:

    • Monoclonal antibodies possess significant self-buffering capacity, particularly at higher concentrations.
    • Self-buffering is a viable and potentially advantageous strategy for developing stable, high-concentration antibody and protein formulations.
    • This approach may reduce the need for external buffering agents, potentially improving formulation stability.