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Antibody structure, instability, and formulation.

Wei Wang1, Satish Singh, David L Zeng

  • 1Pfizer, Inc., Global Biologics, 700 Chesterfield Parkway West, Chesterfield, Missouri 63017, USA. wei.2.wang@pfizer.com

Journal of Pharmaceutical Sciences
|September 26, 2006
PubMed
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The development of therapeutic monoclonal antibodies is rapidly expanding. This review examines antibody structure, instabilities, and formulation strategies to ensure stable and commercially viable antibody pharmaceuticals.

Area of Science:

  • Biopharmaceutical development
  • Protein therapeutics
  • Antibody engineering

Background:

  • Therapeutic monoclonal antibody development is increasing, with over 23 approved in the US and 200+ in development.
  • Antibody pharmaceuticals present unique formulation challenges due to unpredictable solution behavior, despite structural similarities.

Purpose of the Study:

  • To review the structure and function of therapeutic antibodies.
  • To examine mechanisms of physical and chemical instabilities in antibodies.
  • To identify critical attributes for antibody stabilization through formulation development.

Main Methods:

  • Literature review of antibody structure and function.
  • Analysis of physical and chemical degradation pathways.
  • Examination of formulation strategies for antibody stabilization.

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Main Results:

  • Antibodies possess unique solution behaviors impacting pharmaceutical development.
  • Understanding degradation mechanisms is crucial for formulation.
  • Key formulation attributes can enhance antibody stability.

Conclusions:

  • Formulation development is critical for creating stable and commercially viable antibody pharmaceuticals.
  • Addressing antibody instabilities through formulation is essential for therapeutic success.
  • Further research into antibody stabilization is warranted.