56542-65-5

Usage

Uses

Used in Pharmaceutical Industry:
3-Cyano-N-phenylbenzenesulfonamide is used as a functional group in drug design for its ability to contribute to the development of pharmaceutical compounds with desired properties.
Used in Chemical Reactions:
As a reagent, 3-Cyano-N-phenylbenzenesulfonamide is employed in various chemical processes to facilitate specific reactions or transformations.
Used in Medicinal Chemistry Research:
3-Cyano-N-phenylbenzenesulfonamide is utilized in research to explore its potential biological activity, which may lead to the discovery of new therapeutic agents or insights into disease mechanisms.

Upstream product

• 98-95-3 nitrobenzene 
• 150255-96-2 (3‐cyanophenyl)boronic acid 
• 56542-67-7 3-cyanobenzene sulfonyl chloride 
• 62-53-3 aniline 

Relevant academic research and scientific papers

Sequential C-S and S-N Coupling Approach to Sulfonamides

A one-pot three-component reaction involving nitroarenes, (hetero)arylboronic acids, and potassium pyrosulfite leading to sulfonamides was described. A broad range of sulfonamides bearing different reactive functional groups were obtained in good to excellent yields through sequential C-S and S-N coupling that does not require metal catalysts.

Active site mapping of trypsin, thrombin and matriptase-2 by sulfamoyl benzamidines

The benzamidine moiety, a well-known arginine mimetic, has been introduced in a variety of ligands, including peptidomimetic inhibitors of trypsin-like serine proteases. According to their primary substrate specificity, the benzamidine residue interacts with the negatively charged aspartate at the bottom of the S1 pocket of such enzymes. Six series of benzamidine derivatives (1-73) were synthesized and evaluated as inhibitors of two prototype serine proteases, that is, bovine trypsin and human thrombin. As a further target, human matriptase-2, a recently discovered type II transmembrane serine protease, was investigated. Matriptase-2 represents an important regulatory protease in iron homeostasis by down-regulation of the hepcidin expression. Compounds 1-73 were designed to contain a fixed sulfamoyl benzamidine moiety as arginine mimetic and a linker-connected additional substructure, such as a tert-butyl ester, carboxylate or second benzamidine functionality. A systematic mapping approach was performed with these inhibitors to scan the active site of the three target proteases. In particular, bisbenzamidines, able to interact with both the S1 and S3/S4 binding sites, showed notable affinity. In branched bisbenzamidines 66-73 containing a third hydrophobic residue, opposite effects of the stereochemistry on trypsin and thrombin inhibition were observed.