ArticleJournal of the American Chemical Society2025
Ligand-Directed Site-Selective Cysteine Bioconjugation of the KELCH Domain of KEAP1 with Hypervalent Iodine Reagents.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Chemical reactions for the ligand-directed modification of native proteins.Chemical Society reviews · 2026Review
- Progress and challenges in traceless ligand-directed labelling chemistry.Communications chemistry · 2026Review
- Toward Precision Bioconjugation: Chemical Strategies for Site-Selective Cysteine Conjugation.Precision chemistry · 2026Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Affinity-driven reactions have allowed chemists to perform site-selective modifications of native proteins. By combining the high cysteine chemoselectivity of hypervalent iodine-based ethynylbenziodoxolones (EBXs) with the site selectivity of peptide ligands known to inhibit protein-protein interactions, we achieved site-selective labeling of Cys434 in the KELCH domain of Kelch-like epichlorohydrin-associated protein 1 (KEAP1), a key protein in the regulation of oxidative stress. EBXs could be used either as traceless reagents with release of the peptide ligand to introduce reactive handles such as azides or alkynes or as covalent reagents leading to the formation of peptide-protein adducts, which could be cleaved in a separated step.
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