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- W4386989180 abstract "The value of correlating global α-relaxations with long term protein stability after freeze-drying is inconsistently reported. This study aims to clarify whether and to what extend the long term stability of a freeze-dried protein formulation can be predicted with this method. For this purpose, the α-relaxation parameter τβ [h] of freshly prepared freeze-dried products is obtained by isothermal microcalorimetry. The concept is, that molecular movements in the amorphous matrix are strongly reduced in cakes with longer relaxation time and the product should therefore be more resistant against aggregation. To increase τβ in comparison to a conventional freeze-drying cycle, aggressive drying cycles including structural collapse of the product as well as tempering protocols after freeze-drying are applied. The τβ values are correlated with the aggregation rate of a freeze-dried IgG1 monoclonal antibody measured with high performance size exclusion chromatography. The antibody was used in its market formulation and 6 further compositions. A weak correlation between α-relaxation times and IgG1 aggregation was found. A higher mobility level through increased residual moisture helped to improve the correlation." @default.
- W4386989180 created "2023-09-24" @default.
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- W4386989180 date "2023-11-01" @default.
- W4386989180 modified "2023-10-11" @default.
- W4386989180 title "Possibilities and limitations of α-relaxation data of amorphous freeze-dried cakes to predict long term IgG1 antibody stability" @default.
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- W4386989180 doi "https://doi.org/10.1016/j.ijpharm.2023.123445" @default.
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