Journal
JOURNAL OF PHARMACEUTICAL SCIENCES
Volume 98, Issue 9, Pages 3247-3264Publisher
ELSEVIER SCIENCE INC
DOI: 10.1002/jps.21834
Keywords
immunology; protein aggregation; protein formulation; protein; structure; transgenics; protein folding/refolding
Funding
- BaroFold, Inc.
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Aggregation of recombinant therapeutic protein products is a concern due to their potential to induce immune responses. We examined the immunogenicity of protein aggregates in commercial formulations of recombinant human growth hormone produced by freeze-thawing or agitation, two stresses commonly encountered during manufacturing, shipping and handling of therapeutic protein products. In addition, we subjected each preparation to high-pressure treatment to reduce the size and concentration of aggregates present in the samples. Aggregates existing in a commercial formulation, as well as aggregates induced by freeze-thawing and agitation stresses enhanced immunogenicity in one or more mouse models. The use of high-pressure treatment to reduce size and concentrations of aggregates within recombinant human growth hormone formulations reduced their overall immunogenicity in agreement with the immunon hypothesis. (c) 2009 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:3247-3264, 2009
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