Issue 77, 2024

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 Mae 2024
Accepted
30 Eost 2024
First published
03 Gwen. 2024
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2024,60, 10740-10743

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, 60, 10740 DOI: 10.1039/D4CC02125H

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