Spotlight on Stability Optimization

Researchers study glycan-induced structural changes in IgG1 to understand how the conserved Fc glycan stabilizes the antibody’s tertiary structure, particularly in the CH2 and hinge regions. These insights are critical for ensuring therapeutic antibody stability during manufacturing and storage, and they inform assessments by revealing how glycan removal or variation can alter structural integrity, antigen binding, and effector function.

Figure Legend: Peptide level HRPF Results. (A) Volcano plot comparing the Log2(Fold Change) against – Log(p-value). Dotted line represents a p-value of 0.01. From this, we can easily identify multiple regions on IgG that change in average solvent accessibility following de-glycosylation. (B) Crystal structure of an IgG decorated to show regions with a significant change in solvent accessibility following the removal of the glycan. Regions in green were detected with no significant change in oxidation. Red peptides became more exposed while blue became more protected after glycan removal.