250714-81-9Relevant articles and documents
Silver-Catalyzed C(sp3)-H Sulfonylation for the Synthesis of Benzyl Sulfones Using Toluene Derivatives and α-Amino Acid Sulfonamides
Kanyiva, Kyalo Stephen,Shibata, Takanori,Uchida, Kanako
, p. 1377 - 1384 (2021/06/06)
We describe a simple and practical protocol for the synthesis of benzyl sulfones using readily available toluene derivatives and α-amino acid sulfonamides. The reaction proceeds to afford a broad range of benzyl sulfones in moderate to high yields under silver catalysis. The mechanism possibly involves a Minisci-type formation of α-aminoalkyl radical, homolytic cleavage of a N-S bond to generate a sulfonyl radical, and coupling of sulfonyl radical with a benzyl radical formed via hydrogen abstraction by sulfate anion radical. The practicality of the present reaction is demonstrated by a gram-scale synthesis and one-step synthesis of anticancer-active compound. The mechanism studies are conducted using radical scavengers and deuterated toluene.
Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors
Nuti, Elisa,Cuffaro, Doretta,D'Andrea, Felicia,Rosalia, Lea,Tepshi, Livia,Fabbi, Marina,Carbotti, Grazia,Ferrini, Silvano,Santamaria, Salvatore,Camodeca, Caterina,Ciccone, Lidia,Orlandini, Elisabetta,Nencetti, Susanna,Stura, Enrico A.,Dive, Vincent,Rossello, Armando
supporting information, p. 1626 - 1637 (2016/09/03)
Matrix metalloproteinase-12 (MMP-12) can be considered an attractive target to study selective inhibitors useful in the development of new therapies for lung and cardiovascular diseases. In this study, a new series of arylsulfonamide carboxylates, with increased hydrophilicity resulting from conjugation with a β-N-acetyl-d-glucosamine moiety, were designed and synthesized as MMP-12 selective inhibitors. Their inhibitory activity was evaluated on human MMPs by using the fluorimetric assay, and a crystallographic analysis was performed to characterize their binding mode. Among these glycoconjugates, a nanomolar MMP-12 inhibitor with improved water solubility, compound 3 [(R)-2-(N-(2-(3-(2-acetamido-2-deoxy-β-d-glucopyranosyl)thioureido)ethyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid], was identified.
Protease inhibitors. Part 7: Inhibition of Clostridium histolyticum collagenase with sulfonylated derivatives of L-valine hydroxamate
Supuran, Claudiu T.,Scozzafava, Andrea
, p. 67 - 76 (2007/10/03)
Sulfonylated L-valine hydroxamate derivatives were obtained by reaction of alkyl/arylsulfonyl halides with the title amino acid, followed by treatment with benzyl chloride, and conversion of the COOH moiety to the CONHOH group. Other derivatives were obtained by reaction of N-benzyl-L- valine with arylisocyanates, arylsulfonylisocyanates or benzoylisothiocyanate, followed by the similar conversion of the COOH into the CONHOH moiety, with hydroxylamine in the presence of carbodiimides. The obtained compounds were assayed as inhibitors of the Clostridium histolyticum collagenase, ChC (EC 3.4.24.3), a zinc enzyme which degrades triple helical collagen. The hydroxamate derivatives were generally 100-500 times more active than the corresponding carboxylates. In the series of synthesized derivatives, substitution patterns leading to best ChC inhibitors were those involving perfluoroalkylsulfonyl- and substituted-arylsulfonyl moieties, such as pentafluorophenylsulfonyl; 3- and 4-protected-aminophenylsulfonyl-; 3- and 4-carboxyphenylsulfonyl-; 3-trifluoromethylphenylsulfonyl; or 1- and 2- naphthyl among others. Similarly to the matrix metalloproteinase hydroxamate inhibitors, ChC inhibitors of the type reported here must incorporate hydrophobic moieties at the P(2') and P(3') subsites, in order to achieve tight binding to the enzyme. Such compounds might lead to drugs useful in the treatment corneal bacterial keratitis. (C) 2000 Elsevier Science B.V.
