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- W2081212616 abstract "The freeze–drying behavior of three model proteins, namely, lysozyme, BSA, and IgG, has been studied using a variety of techniques under two different primary drying conditions (shelf temperatures of −25°C and +25°C, respectively) in an amorphous formulation. Manometric temperature measurements were used to characterize product temperature (T pr), sublimation rates, and product resistance (R p) during primary drying. Biophysical techniques such as circular dichroism, fluorescence, and Fourier transform infrared spectroscopy were used to study protein conformation. Size exclusion chromatography was used to monitor the formation of high-molecular-weight species (HMWS) over time on storage, and cake morphology was studied using scanning electron microscopy. The differences in the freeze–drying behavior of the three proteins were more evident at higher protein concentrations, where the protein significantly influences the behavior of the formulation matrix. However, these differences were minimized in the aggressive mode and were insignificant at lower protein concentrations where excipients dominated the freeze–drying behavior. Differences in cake morphology were observed between the two drying conditions employed as well as between the three proteins studied. The stability and the protein structure, however, were equivalent for the protein cakes generated using the two different primary drying conditions." @default.
- W2081212616 created "2016-06-24" @default.
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- W2081212616 date "2010-11-06" @default.
- W2081212616 modified "2023-10-07" @default.
- W2081212616 title "Characterizing the Freeze–Drying Behavior of Model Protein Formulations" @default.
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- W2081212616 doi "https://doi.org/10.1208/s12249-010-9530-9" @default.
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