ArticleAnalytical and bioanalytical chemistry2018
Development of an LC-MS/MS peptide mapping protocol for the NISTmAb.
Article in Analytical and bioanalytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Protein Therapeutic Quality Control Using Multi-Attribute Method (MAM): Challenges and Current Practice in cGMP Environments.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Relative Quantitative Analysis of Site-Specific N-Linked Glycosylation in Hyperglycosylated Interferon-β via Mass Spectrometry.International journal of molecular sciences · 2026Article
- Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.Nature methods · 2026Review
- Rapid Antibody Structural Characterization and Quantification via Microdroplet Trypsin Digestion.Journal of the American Society for Mass Spectrometry · 2026Article
- Computational analysis reveals non-consensus N-glycosylation sequons in antibody Fab region.mAbs · 2025Article
- Characterization of a NovelInternational journal of molecular sciences · 2025Article
- Peptide Mapping for Sequence Confirmation of Therapeutic Proteins and Recombinant Vaccine Antigens by High-Resolution Mass Spectrometry: Software Limitations, Pitfalls, and Lessons Learned.International journal of molecular sciences · 2025Article
- Direct In-Bone Protein Digestion With Subsequent LC Separation and Trap Ion Mobility MS Detection of Released Peptides as an Effective Tool for the Proteomic Characterization of Bone Tissues.Journal of separation science · 2025Article
- High-Throughput Monoclonal Antibody Peptide Mapping Using 15-s HPLC Gradients Coupled with Cyclic Ion Mobility-Mass Spectrometry.Analytical chemistry · 2025Article
- NIST Biomanufacturing Reference Materials: Development, Applications, and Impact.Bridge (Washington, D.C. : 1969) · 2025Article
- A Novel Peptide Mapping Method Utilizing Cysteine as a Reducing Agent.Pharmaceutical research · 2025Article
- Clean and Complete Protein Digestion with an Autolysis Resistant Trypsin for Peptide Mapping.Journal of proteome research · 2024Article
- "Small is beautiful" - Examining reliable determination of low-abundant therapeutic antibody glycovariants.Journal of pharmaceutical analysis · 2024Article
- Comparison of N-Glycopeptide to Released N-Glycan Abundances and the Influence of Glycopeptide Mass and Charge States on N-Linked Glycosylation of IgG Antibodies.Journal of proteome research · 2024Article
- Quantification of SARS-CoV-2 monoclonal IgG mass fraction by isotope dilution mass spectrometry.Analytical and bioanalytical chemistry · 2024Article
- An Overview of Biosimilars-Development, Quality, Regulatory Issues, and Management in Healthcare.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Addressing Acid-Catalyzed Deamidation and the Solubility of Hydrophobic Peptides in Multi-Attribute Method Workflows.Analytical chemistry · 2023Article
- Combination of On-Line and Off-Line Two-Dimensional Liquid Chromatography-Mass Spectrometry for Comprehensive Characterization of mAb Charge Variants and Precise Instructions for Rapid Process Development.International journal of molecular sciences · 2023Article
- Multi-Attribute Monitoring Method for Process Development of Engineered Antibody for Site-Specific Conjugation.Journal of the American Society for Mass Spectrometry · 2023Article
- Oligonucleotide mapping via mass spectrometry to enable comprehensive primary structure characterization of an mRNA vaccine against SARS-CoV-2.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide mapping is a component of the analytical toolbox used within the biopharmaceutical industry to aid in the identity confirmation of a protein therapeutic and to monitor degradative events such as oxidation or deamidation. These methods offer the advantage of providing site-specific information regarding post-translational and chemical modifications that may arise during production, processing or storage. A number of such variations may also be induced by the sample preparation methods themselves which may confound the ability to accurately evaluate the true modification levels. One important focus when developing a peptide mapping method should therefore be the use of sample preparation conditions that will minimize the degree of artificial modifications induced. Unfortunately, the conditions that are amenable to effective reduction, alkylation and digestion are often the same conditions that promote unwanted modifications. Here we describe the optimization of a tryptic digestion protocol used for peptide mapping of the NISTmAb IgG1κ which addresses the challenge of balancing maximum digestion efficiency with minimum artificial modifications. The parameters on which we focused include buffer concentration, digestion time and temperature, as well as the source and type of trypsin (recombinant vs. pancreatic; bovine vs porcine) used. Using the optimized protocol we generated a peptide map of the NISTmAb which allowed us to confirm its identity at the level of primary structure. Graphical abstract Peptide map of the NISTmAb RM 8671 monoclonal antibody. Tryptic digestion was performed using an optimized protocol and followed by LC-UV-MS analysis. The trace represents the total ion chromatogram. Each peak was mapped to peptides identified using mass spectrometry data.
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