Middle-Down Mass Spectrometry Characterization of Monoclonal Antibody Enabled by Electron-Activated Dissociation on a Time-of-Flight Platform: A Case Study of Methionine Oxidation PTM Identification and Quantification

Abstract Characterizing post-translational modifications (PTMs) in monoclonal antibody products is critical for ensuring product quality attributes understanding and monitoring. While the bottom-up approach is widely adopted, it suffers from the loss of molecular connectivity and is susceptible to artifact generation. Conversely, top-down approaches face limitations due to the high complexity and poor gas-phase fragmentation of large intact molecules to get site-specific post-translational information profiling. Middle-down MS methods offer a complementary middle-ground approach to both bottom-up and top-down, with broader sequence coverage, and facilitate the simultaneous identification of multiple attributes and proteoforms. In this study, we optimized the electron-activated dissociation (EAD) approach for middle-down sequencing of NISTmAb subunits and present a potential MS and MS/MS strategy to rapidly characterize PTMs on antibodies, using methionine oxidation as an example. Peroxide-stressed and control mAb samples were digested and reduced into subunits using the IdeS enzyme and analyzed via LC-MS, with the optimized MRMHR EAD method. The resulting data enabled high-resolution subunit mass analysis, sequence confirmation, and potential for site-specific oxidation localization. Methionine oxidation localization in NISTmAb was achieved in light chain (M4), Fd’ (M34, M101), and Fc/2 (M16, M122, M192), with these locations confirmed with bottom-up peptide mapping data. Quantification using the Fc/2 subunit enabled detection of oxidation levels up to 1% relative, with strong correlation (R2 > 0.99) between expected and observed values using MS1 data. This middle-down electron-activated dissociation (EAD) approach provides a potential method for site-specific characterization of PTMs in antibody products, offering valuable complementary mapping to support formulation development and production.

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Journal
Analytical Chemistry
Published
2026-09-29
DOI
https://doi.org/10.1021/acs.analchem.6c03432
Primary Topic
Mass Spectrometry Techniques and Applications
Type
article
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Middle-Down Mass Spectrometry Characterization of Monoclonal Antibody Enabled by Electron-Activated Dissociation on a Time-of-Flight Platform: A Case Study of Methionine Oxidation PTM Identification and Quantification

Leigh Donnellan, Abdulafeez Akinloye, Parul Mittal, Mark R. Condina et al.
Analytical Chemistry
Mass Spectrometry Techniques and Applications
article

Middle-Down Mass Spectrometry Characterization of Monoclonal Antibody Enabled by Electron-Activated Dissociation on a Time-of-Flight Platform: A Case Study of Methionine Oxidation PTM Identification and Quantification

Leigh Donnellan, Abdulafeez Akinloye, Parul Mittal, Mark R. Condina, Peter Hoffmann, Mariam Nassiri, Alok Shah, Nathan Edwards, Clifford Young
article en

Abstract

Abstract Characterizing post-translational modifications (PTMs) in monoclonal antibody products is critical for ensuring product quality attributes understanding and monitoring. While the bottom-up approach is widely adopted, it suffers from the loss of molecular connectivity and is susceptible to artifact generation. Conversely, top-down approaches face limitations due to the high complexity and poor gas-phase fragmentation of large intact molecules to get site-specific post-translational information profiling. Middle-down MS methods offer a complementary middle-ground approach to both bottom-up and top-down, with broader sequence coverage, and facilitate the simultaneous identification of multiple attributes and proteoforms. In this study, we optimized the electron-activated dissociation (EAD) approach for middle-down sequencing of NISTmAb subunits and present a potential MS and MS/MS strategy to rapidly characterize PTMs on antibodies, using methionine oxidation as an example. Peroxide-stressed and control mAb samples were digested and reduced into subunits using the IdeS enzyme and analyzed via LC-MS, with the optimized MRMHR EAD method. The resulting data enabled high-resolution subunit mass analysis, sequence confirmation, and potential for site-specific oxidation localization. Methionine oxidation localization in NISTmAb was achieved in light chain (M4), Fd’ (M34, M101), and Fc/2 (M16, M122, M192), with these locations confirmed with bottom-up peptide mapping data. Quantification using the Fc/2 subunit enabled detection of oxidation levels up to 1% relative, with strong correlation (R2 > 0.99) between expected and observed values using MS1 data. This middle-down electron-activated dissociation (EAD) approach provides a potential method for site-specific characterization of PTMs in antibody products, offering valuable complementary mapping to support formulation development and production.

Analytical Chemistry
Adelaide University (AU), The University of Adelaide (AU)
Openalex Percentile: Top 23%
Mass Spectrometry Techniques and Applications
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