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 Maijs 2024
Accepted
30 Aug. 2024
First published
03 Sept. 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

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements