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.

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

Supplementary files

Article information

Article type
Communication
Submitted
02 5 2024
Accepted
30 8 2024
First published
03 9 2024
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2024, Advance Article

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

F. C. Liu, J. Lee, T. Pedrete, E. M. Panczyk, S. Pengelley and C. Bleiholder, Chem. Commun., 2024, Advance Article , DOI: 10.1039/D4CC02125H

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