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.

SUBMITTER: Liu FC 

PROVIDER: S-EPMC11381966 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature