Measuring Aggregation Propensity of a Protein using SUPR-CM

Overview

Aggregation is a major challenge in biologics development, and can be assessed using isothermal chemical denaturation.
Gibbs Free Energy values determined for different concentrations of protein using SUPR-CM.
High-throughput capabilities of SUPR-CM allowed for rapid processing of samples.
Aggregation propensity measured for the same protein in two different buffers (phosphate and acetate).
Evidence showing phosphate significantly increases propensity for the unfolded protein to aggregate.
Acetate buffer showed no statistically significant change in ΔG° values, with over 4x reduction in aggregation propensity when compared to the phosphate samples.

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