I&EC 47 |
| The aggregation of pharmaceutical proteins is a significant concern in processing, storage and delivery operations. Real-time and accelerated stability studies can provide helpful information on tendency to aggregate under specific conditions, but take "real-time" to execute and use elevated temperatures that do not represent anticipated solution condition, respectively. We have used self-interaction chromatography (SIC) to provide insight into the tendency of proteins to self-associate in terms of second virial coefficients and corresponding equilibrium unfolding studies to provide insight into tendency to unfold in terms of unfolding free energies. We have further used these second virial coefficients and unfolding free energies to inform a lumped kinetic model for protein aggregation that can be compared to real-time and accelerated stability data. We report on our comparison of model predictions to physical stability data for two model pharmaceutical proteins, bovine growth hormone and human growth hormone. |
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Industrial and Engineering Chemistry Divisional Fellow Award Symposium - Dr. Ruben Carbonell
1:30 PM-4:50 PM, Monday, April 7, 2008 Morial Convention Center -- Rm. 231, Oral
Division of Industrial & Engineering Chemistry |