Application Note: Measuring Aggregation Propensity of a Protein using SUPR-CM
Aggregation is a major challenge in biologics development, and can be assessed using isothermal chemical denaturation. In this application note, theGibbs Free Energy values were determined for different concentrations of protein, in two different buffers, using SUPR-CM intrinsic fluorescence platereader. SUPR-CM is ideal for this application due to its high-throughput capabilities. By measuring the change in Gibbs Free Energy with protein concentration, the degree of aggregation propensity was measured. Comparison between samples in phosphate and acetate buffers showed that acetate buffer induced less propensity to aggregate than phosphate buffer.