Structural Heterogeneity of the Humanised IgGk NIST Monoclonal Antibody Probed by Tandem-Trapped Ion Mobility Spectrometry and Mobility-Resolved Collision-induced Unfolding.

Investigating the structural heterogeneity of monoclonal antibodies is crucial to achieving optimal therapeutic outcomes. We show that tandem-trapped ion mobility spectrometry enables collision-induced unfolding measurements of antibody subpopulations. Our data suggest that such non-ensemble measurements will improve the structural characterisation of complex biotherapeutics such as multivalent antibodies.