ArticleAnalytical and bioanalytical chemistry2013
Top-down MS for rapid methionine oxidation site assignment in filgrastim.
Article in Analytical and bioanalytical chemistry, 2013. 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, 32 citations in OpenAlex.
- Comparability of biosimilar filgrastim with originator filgrastim: protein characterization, pharmacodynamics, and pharmacokinetics.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2015Trial
- Demonstration of Physicochemical and Functional Similarity of Biosimilar Pegfilgrastim-cbqv to Pegfilgrastim.Drugs in R&D · 2024Article
- Photo-Oxidation of Therapeutic Protein Formulations: From Radical Formation to Analytical Techniques.Pharmaceutics · 2021Review
- Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy.Analytical chemistry · 2020Article
- Article
- Quality Comparison of Biosimilar and Copy Filgrastim Products with the Innovator Product.Pharmaceutical research · 2018Article
- An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes.Nature chemistry · 2018Article
- Complex Nature of Protein Carbonylation Specificity After Metal-Catalyzed Oxidation.Pharmaceutical research · 2017Article
- Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges.Biomolecules · 2015Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein therapeutics have emerged as a major new class of pharmaceuticals. One important shelf-life-limiting factor of biopharmaceuticals is methionine oxidation, and therefore, it is important that analytical methods are able to thoroughly characterize all possible oxidized variants. Here, we present a fast and sensitive method to perform online methionine oxidation site assignment using granulocyte colony-stimulating factor (filgrastim) as a model. The method is based on top-down MS using the all-ion fragmentation mode of the Exactive benchtop mass spectrometer. Conditions that provide information on the intact mass of the protein as well as on fragment ions that allow unambiguous site assignment of methionine oxidation in filgrastim variants as low as 0.12% of total peak area in a chromatographic time scale were identified. Using this method, we performed methionine oxidation site assignment in H2O2-stressed filgrastim and in filgrastim which was stored at intended conditions, respectively. We show that the relative abundance of oxidation species observed in filgrastim stored under intended conditions differs strikingly from the oxidized species observed after H2O2 stress. Additionally, we report an oxidized filgrastim variant that has not been previously described in the literature.
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