ArticleAnalytical chemistry2019
Structural Analysis of Monoclonal Antibodies by Ultrahigh Resolution MALDI In-Source Decay FT-ICR Mass Spectrometry.
Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- Native Top-Down Mass Spectrometry Combined with High-Resolution Charge Variant Analysis of Trastuzumab Originator and Biosimilars.Journal of the American Society for Mass Spectrometry · 2026Article
- The Synthesis and Anticancer Activity of the Trastuzumab-Doxorubicin Antibody-Drug Conjugate Using Strain-Promoted Alkyne-Azide Coupling.ACS omega · 2026Article
- Top-Down and Middle-Down Mass Spectrometry of Antibodies.Molecular & cellular proteomics : MCP · 2025Review
- Improving Top-Down Sequence Coverage with Targeted Fragment Matching.Journal of the American Society for Mass Spectrometry · 2024Article
- Enhanced Payload Localization in Antibody-Drug Conjugates Using a Middle-Down Mass Spectrometry Approach with Proton Transfer Charge Reduction.Analytical chemistry · 2024Article
- Towards a universal method for middle-down analysis of antibodies via proton transfer charge reduction-Orbitrap mass spectrometry.Analytical and bioanalytical chemistry · 2024Article
- Direct glycosylation analysis of intact monoclonal antibodies combining ESI MS of glycoforms and MALDI-in source decay MS of glycan fragments.Communications chemistry · 2024Article
- Mass Spectrometry Strategies forCells · 2024Review
- Improved characterization of trastuzumab deruxtecan with PTCR and internal fragments implemented in middle-down MS workflows.Analytical and bioanalytical chemistry · 2024Article
- Mass spectrometry characterization of antibodies at the intact and subunit levels: from targeted to large-scale analysis.International journal of mass spectrometry · 2023Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- rMSIfragment: improving MALDI-MSI lipidomics through automated in-source fragment annotation.Journal of cheminformatics · 2023Article
- Revealing charge heterogeneity of stressed trastuzumab at the subunit level.Analytical and bioanalytical chemistry · 2023Article
- Analytical Techniques for the Characterization and Quantification of Monoclonal Antibodies.Pharmaceuticals (Basel, Switzerland) · 2023Review
- 193 nm Ultraviolet Photodissociation for the Characterization of Singly Charged Proteoforms Generated by MALDI.Journal of the American Society for Mass Spectrometry · 2023Article
- MALDI-TOF-MS-Based Identification of Monoclonal Murine Anti-SARS-CoV-2 Antibodies within One Hour.Antibodies (Basel, Switzerland) · 2022Article
- Glycan and Protein Analysis of Glycoengineered BacterialAnalytical chemistry · 2022Article
- Applications and advancements of FT-ICR-MS for interactome studies.Mass spectrometry reviews · 2022Review
- Native Liquid Chromatography and Mass Spectrometry to Structurally and Functionally Characterize Endo-Xylanase Proteoforms.International journal of molecular sciences · 2022Article
- Rapid structural discrimination of IgG antibodies by multicharge-state collision-induced unfolding.RSC advances · 2021Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emergence of complex protein therapeutics in general and monoclonal antibodies (mAbs) in particular have stimulated analytical chemists to develop new methods and strategies for their structural characterization. Mass spectrometry plays a key role in providing information on the primary amino acid sequence, post-translational modifications, and other structure characteristics that must be monitored during the manufacturing process and subsequent quality control assessment. In this study, we present a novel method that allows structural characterization of mAbs based on MALDI in-source decay (ISD) fragmentation, coupled with Fourier transform ion cyclotron resonance (FT-ICR) MS. The method benefits from higher resolution of absorption mode FT mass spectra, compared to magnitude mode, which enables simultaneous identification of ISD fragments from both the heavy and light chains with a higher confidence in a wide mass range up to m/ z 13 500. This method was applied to two standard mAbs, namely NIST mAb and trastuzumab, in preparation for method application in an interlaboratory study on mAbs structural analysis coordinated by the Consortium for Top-Down Proteomics. Extensive sequence coverage was obtained from the middle-down analysis (IdeS- and GingisKHAN-digested mAbs) that complemented the top-down analysis of intact mAbs. In addition, MALDI FT-ICR MS of IdeS-digested mAbs allowed isotopic-level profiling of proteoforms with regard to heavy chain N-glycosylation.
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