Differential glycosylation does not modulate the conformational heterogeneity of a humanised IgGk NIST monoclonal antibody†
Abstract
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.
- This article is part of the themed collection: 2024 Pioneering Investigators