Charge and Interaction Analysis for Predicting Antibody Formulation Stability

This application note demonstrates how combined measurements of net charge and kD can help us to understand the difference between two formulations with different stability behavior. In this example, although the formulations have the same net charge, secondary effects of asymmetric charge distributions and hydrophobic residues result in the stability differences. This article illustrates how the Wyatt Möbius’ capabilities can be used to gain a more thorough understanding of factors affecting a protein’s stability.