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Structural Heterogeneity of the Humanised IgGk NIST Monoclonal Antibody Probed by Tandem-Trapped Ion Mobility Spectrometry and Mobility-Resolved Collision-induced Unfolding.

02 July 2024, Version 2
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

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 antibody subpopulations. Our data suggest that such non-ensemble measurements will improve the structural characterisation of complex biotherapeutics such as multivalent antibodies.

Keywords

monoclonal antibodies
structural heterogeneity
ion mobility spectrometry/mass spectrometry
Tandem-TIMS
collision-induced unfolding

Supplementary materials

Title
Description
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Title
Supporting Information
Description
mass spectra; comparison of cross-sections by Tandem-TIMS and DTIMS; ensemble CIU spectra; Structure Relaxation Approximation calculation.
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Version History

Jul 02, 2024 Version 2

Version Notes

add Funding agency

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv-2024-7hj35-v2
D O I: 10.26434/chemrxiv-2024-7hj35-v2 [opens in a new tab]

Funding

National Science Foundation
CHE 2305173
National Institutes of Health
R01GM135682

Author’s competing interest statement

S.P. and E.M.P. are employees at Bruker Corporation, which sells timsTOF instruments.

Ethics

The author(s) have declared ethics committee/IRB approval is not relevant to this content

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