期刊
AICHE JOURNAL
卷 68, 期 12, 页码 -出版社
WILEY
DOI: 10.1002/aic.17850
关键词
excipient; extensional flow; polysorbate; protein; rheology
资金
- National Science Foundation [CON-75851]
This study examined the extensional flow properties of protein-excipient solutions using dripping-onto-substrate extensional rheology. The results showed that the identity of the excipient polysorbate (PS) influenced the extensional flow behavior, particularly at moderate total concentrations and small PS:OVA ratios. Undesirable elasticity was observed in ultra-concentrated formulations, and higher PS contents were required to observe these effects compared to analogous polymeric excipients. This research provides insight into the extensional flow stability of new protein-excipient formulations.
While protein medications are promising for treatment of cancer and autoimmune diseases, challenges persist in terms of development and injection stability of high-concentration formulations. Here, the extensional flow properties of protein-excipient solutions are examined via dripping-onto-substrate extensional rheology, using a model ovalbumin (OVA) protein and biocompatible excipients polysorbate 20 (PS20) and 80 (PS80). Despite similar PS structures, differences in extensional flow are observed based on PS identity in two regimes: at moderate total concentrations where surface tension differences drive changes in extensional flow behavior, and at small PS:OVA ratios, which impact the onset of weakly elastic flow behavior. Undesirable elasticity is observed in ultra-concentrated formulations, independent of PS identity; higher PS contents are required to observe these effects than in analogous polymeric excipient solutions. These studies reveal novel extensional flow behaviors in protein-excipient solutions, and provide a straightforward methodology for assessing the extensional flow stability of new protein-excipient formulations.
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