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

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

doi:10.26434/chemrxiv-2024-7hj35

Analytical Chemistry

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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.

08 May 2024, Version 1

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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

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Supporting Information

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mass spectra; comparison of cross-sections by Tandem-TIMS and DTIMS; ensemble CIU spectra; Structure Relaxation Approximation calculation.

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Jul 02, 2024 Version 2

May 08, 2024 Version 1

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The content is available under CC BY NC ND 4.0

DOI

10.26434/chemrxiv-2024-7hj35

Funding

National Science Foundation

CHE 2305173

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

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

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Abstract

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Supplementary materials

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Author’s competing interest statement

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