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Abstract | Cited by

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 subpopulations of a humanised IgGk NIST monoclonal antibody (NISTmAb). Our results indicate that differential glycosylation of NISTmAb does not modulate its conformational heterogeneity.

Graphical abstract: Differential glycosylation does not modulate the conformational heterogeneity of a humanised IgGk NIST monoclonal antibody

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