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

Fanny C. Liu; Jusung Lee; Thais Pedrete; Erin M. Panczyk; Stuart Pengelley; Christian Bleiholder

doi:10.1039/D4CC02125H

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

Fanny C. Liu,

*^a Jusung Lee,

^a Thais Pedrete,

^a Erin M. Panczyk,

^b Stuart Pengelley

^c and Christian Bleiholder

*^ad

Author affiliations

* Corresponding authors

^a Department of Chemistry and Biochemistry, Florida State University, 102 Varsity Way, Tallahassee, Florida, USA
E-mail: cbleiholder@fsu.edu, fliu@fsu.edu

^b Bruker Daltonics, 40 Manning Road, Billerica, MA 01821, USA

^c Bruker Daltonics GmbH&Co, Fahrenheitstrasse 4, Bremen, Germany

^d Institute of Molecular Biophysics, Florida State University, 91 Chieftan Way, Tallahassee, Florida, USA

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.

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Article information

DOI: https://doi.org/10.1039/D4CC02125H
Article type: Communication
Submitted: 02 ៥ 2024
Accepted: 30 ៨ 2024
First published: 03 ៩ 2024
This article is Open Access

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

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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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Chemical Communications

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

Abstract

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

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