Presented by: Joseph Arndt, Ph.D., Senior Scientist, Biogen
Presented Live: November 4, 2015 at the 24th International Light Scattering Colloquium, Santa Barbara, CA
A detailed knowledge of interrelationships between structure and function is a requirement for the development of biologics. Environmental perturbations from the manufacturing process such as temperature, pH, and solute additives can impact higher order structure and stability in solution. In this talk, a case study will be presented in which a neurotrophic protein was rendered inactive, with significantly reduced viscosity, as a result of a commonly used viral inactivation step using low-pH incubation. The structure, oligomerization state, and dynamics of the native and viral inactivated protein were examined using orthogonal light scattering techniques to understand the underlying origin of the activity loss and change in rheological behavior. These studies highlight the structure-function complexity of protein biologics that must be maintained at all stages of the drug development.
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