ArticleJournal of the American Society for Mass Spectrometry2026
Quantitative Mapping of NHS Ester-Protein Reactivity Using Native Top-Down Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Covalent ligands are widely used to label, probe, and modulate proteins, but peptide-centric readouts obscure how modifications colocalize on intact proteoforms. This can limit insight into ligand mechanism, modification stoichiometry, and the architecture of multisite protein conjugates. We present a general native top-down mass spectrometry workflow that quantifies electrophile reactivity directly on intact proteins. Using NHS esters as a model electrophile class, we apply a deconvolution framework to infer differential reactivity at primary amines across promiscuous, multisite modification patterns. The approach preserves full modification connectivity, avoids sample-preparation artifacts associated with denaturation and digestion, and should extend to electrophiles with unknown reactivity. Overall, this framework provides a general platform for designing covalent therapeutics, bioconjugates, and activity-based probes with proteoform-level resolution.
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