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Antibody structure, instability, and formulation
Article first published online: 22 SEP 2006
DOI: 10.1002/jps.20727
Copyright © 2006 Wiley-Liss, Inc.
Total views since August 2010: 5780
Additional Information
How to Cite
Wang, W., Singh, S., Zeng, D. L., King, K. and Nema, S. (2007), Antibody structure, instability, and formulation. J. Pharm. Sci., 96: 1–26. doi: 10.1002/jps.20727
Publication History
- Issue published online: 23 NOV 2006
- Article first published online: 22 SEP 2006
- Manuscript Accepted: 4 JUN 2006
- Manuscript Revised: 17 MAY 2006
- Manuscript Received: 14 MAR 2006
Keywords:
- biotechnology;
- stabilization;
- protein formulation;
- protein aggregation;
- freeze drying/lyophilization
Abstract
The number of therapeutic monoclonal antibody in development has increased tremendously over the last several years and this trend continues. At present there are more than 23 approved antibodies on the US market and an estimated 200 or more are in development. Although antibodies share certain structural similarities, development of commercially viable antibody pharmaceuticals has not been straightforward because of their unique and somewhat unpredictable solution behavior. This article reviews the structure and function of antibodies and the mechanisms of physical and chemical instabilities. Various aspects of formulation development have been examined to identify the critical attributes for the stabilization of antibodies. © 2006 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 96:1–26, 2007