Protein formulation stability - case study
Protein formulation technology is an integral part of drug development. The active ingredients such as a protein must be stable over the shelf life of the product. Conversely it may be possible to modify the shelf life significantly when a change to the active ingredient is made.
Also, thermal stability of the ingredients is a good indicator of protein formulation stability, and may be used as an indicator to predict shelf life of the protein formulation.
A different approach to increasing stability is to modify the protein formulation directly. For example, steric stabilization or modification of the zeta potential of liposomes will influence the overall stability. Often, a solution change (pH, salts, additives) will lead to a significant change in the zeta potential.
On demand presentation on monitoring and predicting protein formulation stability Stability can be defined in various ways from expiration dates to shelf life. The z-average size from dynamic light scattering measurements can be used to monitor time dependent aggregation of protein formulations. The Zeta potential from electrophoretic light scattering is often used to characterize the surface properties of particles, and is influenced by both steric and charge effects.
Application note on Automated size and intensity trend measurements. The ability to automate particle size and scattering intensity trend measurements can be a major advantage in many applications. Processes such as aggregation, sedimentation, solubilization and changes in molecular conformation can be followed by monitoring changes in the size and the scattering of the sample. The Zetasizer Nano range allows automated measurements of particle size and scattering intensity as a function of temperature or time. This application note discusses the types of trend measurements available with examples.