5398-09-4Relevant articles and documents
Practical Electro-Oxidative Sulfonylation of Phenols with Sodium Arenesulfinates Generating Arylsulfonate Esters
Tian, Zhibin,Gong, Qihang,Huang, Tianzeng,Liu, Long,Chen, Tieqiao
, p. 15914 - 15926 (2021/05/04)
A practical and sustainable synthesis of arylsulfonate esters has been developed through electro-oxidation. This reaction employed the stable and readily available phenols and sodium arenesulfinates as the starting materials and took place under mild reaction conditions without additional oxidants. A wide range of arylsulfonate esters including those bearing functional groups were produced in good to excellent yields. This reaction could also be conducted at a gram scale without a decrease of reaction efficiency. Those results well demonstrated the potential synthetic value of this reaction in organic synthesis.
Liganding Functional Tyrosine Sites on Proteins Using Sulfur-Triazole Exchange Chemistry
Brulet, Jeffrey W.,Borne, Adam L.,Yuan, Kun,Libby, Adam H.,Hsu, Ku-Lung
supporting information, p. 8270 - 8280 (2020/05/25)
Tuning reactivity of sulfur electrophiles is key for advancing click chemistry and chemical 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) chemistry 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 versus 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 chemical 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 chemistry with broad applications for chemical proteomics and protein ligand discovery.
Synthetic studies toward spiroleucettadine
Chang, Jonah J.,Chan, Bryan,Ciufolini, Marco A.
, p. 3599 - 3601 (2007/10/03)
Synthetic hydroxydienone precursors to spiroleucettadine and to an isomer thereof resist cyclization to the orthoamide-type functionality present in the proposed structure of the natural product.
