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• W3027742687 startingPage "9086" @default.
• W3027742687 abstract "Programmed cell death-1 (PD-1), an antigen co-receptor on cell surfaces, is one of the conspicuous immune checkpoints. Nivolumab, a monoclonal antibody therapeutic approved by the FDA, binds to PD-1 and efficiently blocks its pathways. In this study, an integrated approach was developed to map the epitope/paratope of PD-1/nivolumab. The approach includes hydrogen–deuterium exchange mass spectrometry (HDX-MS) followed by electron-transfer dissociation (ETD), chemical cross-linking, and molecular docking. HDX-ETD offers some binding-site characterization with amino acid resolution. Chemical cross-linking provides complementary information on one additional epitope (i.e., the BC-loop) and a potential paratope at the N-terminus of the heavy chain. Furthermore, cross-linking identifies another loop region (i.e., the C’D-loop) that undergoes a remote conformational change. The distance restraints derived from the cross-links enable building high-confidence models of PD-1/nivolumab, evaluated with respect to a resolved crystal structure. This integrated strategy is an opportunity to characterize comprehensively other antigen–antibody interactions, to enable the understanding of binding mechanisms, and to design future antibody therapeutics." @default.
• W3027742687 created "2020-05-29" @default.
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• W3027742687 date "2020-05-22" @default.
• W3027742687 modified "2023-10-18" @default.
• W3027742687 title "Epitope and Paratope Mapping of PD-1/Nivolumab by Mass Spectrometry-Based Hydrogen–Deuterium Exchange, Cross-linking, and Molecular Docking" @default.
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• W3027742687 doi "https://doi.org/10.1021/acs.analchem.0c01291" @default.
• W3027742687 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7501946" @default.
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• W3027742687 hasPublicationYear "2020" @default.
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