Applying Raman spectroscopy to design of lyophilization cycles for protein formulation development

摘要

Freeze drying (lyophilization) is widely used for biopharmaceuticals to improve stability during shipping and storage. However, the lyophilization process must be optimized to deliver the best quality and performance of the drug product. The lyophilization steps starts with freezing, where the water is converted to ice and the solutes crystallize or become amorphous. The next step is primary drying, where the ice crystals undergo sublimation under vacuum. The final step is secondary drying under higher vacuum to remove residual water by desorption [1, 2]. Freezing and dehydration during lyophilization can cause conformational changes in the protein structure and determine the polymorphs formed during excipient crystallization.