ArticleJournal of the American Chemical Society2024
Charge Detection Mass Spectrometry Reveals Conformational Heterogeneity in Megadalton-Sized Monoclonal Antibody Aggregates.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed.
- Accurate Sizing and Resolution of Nominal 200 nm Diameter Polystyrene Nanospheres With Charge Detection Mass Spectrometry.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Evaluating Antibody Quality via Simultaneous Size and Charge Measurement with Single Protein Oscillators.Analytical chemistry · 2026Article
- Stress-Induced Antibody Aggregates: Insights from Native SEC-MS with Postcolumn Denaturation.Journal of the American Society for Mass Spectrometry · 2026Article
- Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology.Analytical chemistry · 2025Article
- Adeno-associated virus serotype 9 structural heterogeneity and stability characterized by charge detection mass spectrometry.Molecular therapy. Methods & clinical development · 2025Article
- Effects of Hydration on Transthyretin Conformational Dynamics and Oligomerization.Biochemistry · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Single particle charge detection mass spectrometry enables molecular characterization of lipid nanoparticles and mRNA packaging.Journal of controlled release : official journal of the Controlled Release Society · 2025Article
- Characterizing the Content and Structure of AAV Capsids by Size Exclusion Chromatography and Orbitrap-Based Charge Detection-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Dissecting Hidden Liraglutide Oligomerization Pathways via Direct Mass Technology, Electron-Capture Dissociation, and Molecular Dynamics.Analytical chemistry · 2025Article
- Characterizing Monoclonal Antibody Aggregation Using Charge Detection Mass Spectrometry and Industry Standard Methods.Journal of the American Society for Mass Spectrometry · 2025Article
- Article
- Understanding the Formation Dynamics and Physical Properties of Nanocapsules Using Charge Detection Mass Spectrometry.ACS nano · 2025Article
- High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.Analytical chemistry · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Aggregation of protein-based therapeutics can occur during development, production, or storage and can lead to loss of efficacy and potential toxicity. Native mass spectrometry of a covalently linked pentameric monoclonal antibody complex with a mass of ∼800 kDa reveals several distinct conformations, smaller complexes, and abundant higher-order aggregates of the pentameric species. Charge detection mass spectrometry (CDMS) reveals individual oligomers up to the pentamer mAb trimer (15 individual mAb molecules; ∼2.4 MDa) whereas intermediate aggregates composed of 6-9 mAb molecules and aggregates larger than the pentameric dimer (1.6 MDa) were not detected/resolved by standard mass spectrometry, size exclusion chromatography (SEC), capillary electrophoresis (CE-SDS), or by mass photometry. Conventional quadrupole time-of-flight mass spectrometry (QTOF MS), mass photometry, SEC, and CE-SDS did not resolve partially or more fully unfolded conformations of each oligomer that were readily identified using CDMS by their significantly higher extents of charging. Trends in the charge-state distributions of individual oligomers provides detailed insight into how the structures of compact and elongated mAb aggregates change as a function of aggregate size. These results demonstrate the advantages of CDMS for obtaining accurate masses and information about the conformations of large antibody aggregates despite extensive overlapping
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