Journal
JOURNAL OF PHARMACEUTICAL SCIENCES
Volume 105, Issue 1, Pages 40-49Publisher
ELSEVIER SCIENCE INC
DOI: 10.1002/jps.24705
Keywords
freeze-drying; lyophilization; protein formulation; thermal analysis; glass transition; stability; processing; drying
Ask authors/readers for more resources
This study explored the ability to conduct primary drying during lyophilization at product temperatures above the glass transition temperature of the maximally freeze-concentrated solution (T-g') in amorphous formulations for four proteins from three different classes. Drying above T-g' resulted in significant reductions in lyophilization cycle time. At higher protein concentrations, formulations freeze dried above T-g' but below the collapse temperature yielded pharmaceutically acceptable cakes. However, using an immunoglobulin G type 4 monoclonal antibody as an example, we found that as protein concentration decreased, minor extents of collapse were observed in formulations dried at higher temperatures. No other impacts to product quality, physical stability, or chemical stability were observed in this study among the different drying conditions for the different proteins. Drying amorphous formulations above T-g', particularly high protein concentration formulations, is a viable means to achieve significant time and cost savings in freeze-drying processes. (C) 2016 American Pharmacists Association (R). Published by Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available