ArticleJournal of the American Society for Mass Spectrometry2025
Mass Spectrometry-Driven Epitope Mapping: Application of Diethylpyrocarbonate Covalent Labeling for the Immunotherapeutic Target Programmed Cell Death Protein 1.
Article in Journal of the American Society for Mass Spectrometry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Mass spectrometry-based mapping of conformational epitopes on SARS-CoV-2 antigens targeted by monoclonal antibodies.International journal of biological macromolecules · 2026Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors.
Funding
Abstract
Monoclonal antibodies (mAbs) have revolutionized immuno-oncology, with anti-programmed cell death protein 1 (PD1) mAbs emerging as key therapeutic agents in cancer treatment. This study presents the development and application of diethylpyrocarbonate (DEPC) covalent labeling-mass spectrometry (CL-MS) for detailed epitope mapping of anti-PD1 mAbs on PD1. By using DEPC CL-MS, we aimed to identify precise antibody binding sites on PD1 and benchmark its effectiveness against traditional X-ray crystallography. DEPC CL-MS offers high sensitivity and specificity while requiring less sample preparation and shorter analysis times, typically taking days or less, instead of months. PD1 was individually incubated with either nivolumab or a novel anti-human PD1 mAb (CU-MAB), followed by DEPC labeling, to assess DEPC modification extents under both binding and nonbinding conditions using bottom-up LC-MS/MS. Significant changes in DEPC modification at residues S27, S60, S62, S127, and K131 indicated binding sites and conformational shifts upon antibody interaction. These findings showed strong alignment with crystallography (PD1/nivolumab) and AlphaFold structural predictions (PD1/nivolumab and PD1/CU-MAB), highlighting the value of in-solution CL-MS for confirming AlphaFold predictions. This study underscores DEPC CL-MS as an efficient tool for epitope mapping, offering actionable insights into PD1-antibody interactions to drive therapeutic antibody development.
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What OpenQuestion holds
Registered trials
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.