期刊
INTERNATIONAL JOURNAL OF PHARMACEUTICS
卷 495, 期 1, 页码 608-611出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijpharm.2015.09.031
关键词
PEGylation; HESylation; Freeze-drying; Phase separation; Interferon alpha-2b; Crystallization
A comparison of lyophilized PEGylated and HESylated IFN alpha was carried out to investigate the influence of protein conjugation, lyoprotectants as well as storage temperature on protein stability. Results show that PEG tends to crystallize during freeze-drying, reducing protein stability upon storage. In contrast, HESylation (R) drastically improved the stability over PEGylation by remaining totally amorphous during lyophilization, with and without lyoprotectants while providing a high glass transition temperature of the freeze-dried cakes. (C) 2015 Elsevier B.V. All rights reserved.
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