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Getting the Full Picture: Predicting the Aggregation Propensity of mAbs Using Chemical and Thermal Denaturation on a Single, Fully Automated Platform
The presented data demonstrates that chemical denaturation is a feasible approach to predict the colloidal long-term stability of biologicals. Moreover, changes in G in dependence of the protein concentration can give immediate feedback whether protein aggregation occurs, and can also be used to discriminate between native- and denatured-state aggregation. Knowledge about the aggregation mechanism is vital to design further steps in the development process: Denatured state aggregation can be reduced by excipients which further stabilize protein conformation, while native state aggregation might require different optimization strategies, such as excipients that shield surface-exposed hydrophobic patches in aggregation-promoting sequences, or protein engineering to eliminate such critical sequences entirely (Courtois et al, 2016; Seeliger et al, 2015).
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