Principal Scientist Genentech, Inc. South San Francisco
Developing a stabilized spray-dried formulation for proteins is essential for extending the stability of a dehydrated drug product and enhancing various drug delivery applications. However, the hygroscopic nature of amorphous trehalose makes it prone to recrystallization, which can negatively affect protein stability in the solid state. This study addresses this challenge by employing 2-hydroxypropyl-ꞵ-cyclodextrin (HPꞵCD) in combination with trehalose to enhance the physical stability of spray-dried proteins. Our results demonstrate that HPꞵCD effectively inhibits trehalose recrystallization, thereby preserving the stability of monoclonal antibodies (mAbs) upon exposure to high temperatures and humidity conditions. Analytical techniques such as PXRD, FTIR, and SEC confirm that the combination of HPβCD and trehalose prevents protein aggregation and maintains an amorphous structure under stress conditions. These findings highlight the potential of HPβCD as a crystallization inhibitor, providing a robust formulation approach to improve the stability and efficacy of spray-dried therapeutic proteins.
Learning Objectives:
Upon completion, participant will be able to learn key considerations for formulation development of therapeutic monoclonal antibodies as spray-dried solids
Upon completion, participant will be able to design experiments for assessing solid-state protein stability.
Upon completion, participant will be able to understand the importance of protein stability for drug development.
