Brulet, Jeffrey W. published the artcileLiganding Functional Tyrosine Sites on Proteins Using Sulfur-Triazole Exchange Chemistry, Name: Isonicotinamide, the publication is Journal of the American Chemical Society (2020), 142(18), 8270-8280, database is CAplus and MEDLINE.
Tuning reactivity of sulfur electrophiles is key for advancing click chem. and chem. probe discovery. To date, activation of the sulfur electrophile for protein modification has been ascribed principally to stabilization of a fluoride leaving group (LG) in covalent reactions of sulfonyl fluorides and arylfluorosulfates. We recently introduced sulfur-triazole exchange (SuTEx) chem. to demonstrate the triazole as an effective LG for activating nucleophilic substitution reactions on tyrosine sites of proteins. Here, we probed tunability of SuTEx for fragment-based ligand discovery by modifying the adduct group (AG) and LG with functional groups of differing electron-donating and -withdrawing properties. We discovered the sulfur electrophile is highly sensitive to the position of modification (AG vs. LG), which enabled both coarse and fine adjustments in solution and proteome activity. We applied these reactivity principles to identify a large fraction of tyrosine sites (~30%) on proteins (~44%) that can be liganded across >1500 probe-modified sites quantified by chem. proteomics. Our proteomic studies identified noncatalytic tyrosine and phosphotyrosine sites that can be liganded by SuTEx fragments with site specificity in lysates and live cells to disrupt protein function. Collectively, we describe SuTEx as a versatile covalent chem. with broad applications for chem. proteomics and protein ligand discovery.
Journal of the American Chemical Society published new progress about 1453-82-3. 1453-82-3 belongs to amides-buliding-blocks, auxiliary class Pyridine,Amine,Amide, name is Isonicotinamide, and the molecular formula is C6H6N2O, Name: Isonicotinamide.
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