ArticlemAbs
Comprehensive characterization of higher order structure changes in methionine oxidized monoclonal antibodies via NMR chemometric analysis and biophysical approaches.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- 2D NMR assessment of structural consistency and functional relationships in monoclonal antibodies.mAbs · 2026Article
- Review of Quality Attributes and Analytical Methods Used for Comparative Analytical Assessment of Monoclonal Antibodies as Part of Successful Biosimilar Approvals in the United States and European Union.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Methyl-specific NMR of therapeutic antibodies: cost-effective isotopic labeling strategies in CHO cells for high-resolution structural characterization.Journal of biomolecular NMR · 2026Article
- Stereochemical and Structural Characterization of Methionine Oxidation in the IgG1 Fc Region by Integrated NMR and LC-MS Analysis.Analytical chemistry · 2026Article
- Article
- Middle-Down Nuclear Magnetic Resonance for Therapeutic Monoclonal Antibody Glycan Profiling.Current protocols · 2025Article
- The Structural Fingerprint of Therapeutic Monoclonal Antibodies Determined Using a Combination of Near-UV Circular Dichroism and Statistical Approach for Comparative Analysis.Analytical chemistry · 2025Article
- Investigation into the pharmacodynamics and pharmacokinetics of recombinant human interferon alfa-2b vaginal suppository following process optimization in chinese rhesus macaque.Scientific reports · 2025Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The higher order structure (HOS) of monoclonal antibodies (mAbs) is an important quality attribute with strong contribution to clinically relevant biological functions and drug safety. Due to the multi-faceted nature of HOS, the synergy of multiple complementary analytical approaches can substantially improve the understanding, accuracy, and resolution of HOS characterization. In this study, we applied one- and two-dimensional (1D and 2D) nuclear magnetic resonance (NMR) spectroscopy coupled with chemometric analysis, as well as circular dichroism (CD), differential scanning calorimetry (DSC), and fluorescence spectroscopy as orthogonal methods, to characterize the impact of methionine (Met) oxidation on the HOS of an IgG1 mAb. We used a forced degradation method involving concentration-dependent oxidation by peracetic acid, in which Met oxidation is site-specifically quantified by liquid chromatography-mass spectrometry. Conventional biophysical techniques report nuanced results, in which CD detects no change to the secondary structure and little change in the tertiary structure. Yet, DSC measurements show the destabilization of Fab and Fc domains due to Met oxidation. More importantly, our study demonstrates that 1D and 2D NMR and chemometric analysis can provide semi-quantitative analysis of chemical modifications and resolve localized conformational changes with high sensitivity. Furthermore, we leveraged a novel
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.