ArticlemAbs
Understanding the impacts of dual methionine oxidations in complementarity-determining regions on the structure of monoclonal antibodies.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Structural insights into antibody-antibody interactions in sandwich ELISA: implications for assay development and performance.Analytical and bioanalytical chemistry · 2026Article
- Measurement of the absolute mass concentration of antigen-specific serum IgG via quantitative Western blotting.Analytical biochemistry · 2026Article
- Mechanistic insight into the oxidative degradation of monoclonal antibodies: relevance to developability and the design of stable pharmaceutical formulations.Biochemical Society transactions · 2026Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methionine oxidation can substantially alter the structure and functionality of monoclonal antibodies (mAbs), especially when it occurs in the complementarity-determining regions (CDRs). It is imperative to fully understand the effects of methionine oxidation because these modifications can affect the binding affinity, stability, and immunogenicity of mAbs. Moreover, the presence of multiple methionines in close proximity within the amino acid sequence increases the complexity of accurate characterization, and sophisticated analytical methods are required to detect these modifications. In this study, we used hydrogen deuterium exchange mass spectrometry (HDX-MS) and homology modeling to investigate the effects of dual methionine oxidations (heavy chain (HC) Met111 and Met115) within a single CDR on the structure of a mAb. Our findings reveal that the solvent-accessible methionine (HC Met111) is more prone to oxidation, but such a modification does not result in conformational changes in the mAb. In contrast, the methionine (HC Met115) at the V
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