23761-01-5

Upstream product

• 103-71-9 phenyl isocyanate 
• 63-74-1 sulfanilamide 
• 1773-42-8 4-(chlorosulfonyl)phenyl isocyanate 
• 62-53-3 aniline 

Downstream Products

• 1396126-74-1 C₁₆H₁₃N₃O₅S 
• 1396127-05-1 C₁₈H₁₂F₃N₃O₆S 
• 1396127-30-2 C₂₃H₁₇N₃O₅S 
• 1396127-32-4 C₂₃H₁₅F₂N₃O₅S 
• 1396127-56-2 C₁₈H₁₂F₃N₅O₄S 

Relevant academic research and scientific papers

Synthesis and biological evaluation of new barbituric and thiobarbituric acid fluoro analogs of benzenesulfonamides as antidiabetic and antibacterial agents

A novel series of benzenesulfonamide derivatives of barbituric and thiobarbituric acids (2-12) were synthesized by condensation and cyclization reactions of various ureido and thioureido derivatives of sulfanilamides. Different substituents have been inco

NOVEL SULFONAMIDE COMPOUNDS FOR INHIBITION OF METASTATIC TUMOR GROWTH

Therapeutic sulfonamide compounds with the formula R-Q-Ar-SO2NH2 are disclosed, wherein R is an aryl, hetaryl, alkyl or cycloalkyl group, Q is the group -L(CH2)n-, wherein n = 0,1 or 2 and L is the group - NHCXN

Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis

A series of ureido-substituted benzenesulfonamides was prepared that showed a very interesting profile for the inhibition of several human carbonic anhydrases (hCAs, EC 4.2.1.1), such as hCAs I and II (cytosolic isoforms) and hCAs IX and XII (transmembrane, tumor-associated enzymes). Excellent inhibition of all these isoforms has been observed with various members of the series, depending on the substitution pattern of the urea moiety. Several low nanomolar CA IX/XII inhibitors also showing good selectivity for the transmembrane over the cytosolic isoforms have been discovered. One of them, 4-{[(3′- nirophenyl)carbamoyl]amino}benzenesulfonamide, significantly inhibited the formation of metastases by the highly aggressive 4T1 mammary tumor cells at pharmacologic concentrations of 45 mg/kg, constituting an interesting candidate for the development of conceptually novel antimetastatic drugs.

Inhibition of β-carbonic anhydrases with ureido-substituted benzenesulfonamides

A series of sulfonamides was prepared by reaction of sulfanilamide with aryl/alkyl isocyanates. The ureido-substituted benzenesulfonamides showed a very interesting profile for the inhibition of several carbonic anhydrases (CAs, EC 4.2.1.1) such as the human hCA II and three β-CAs from pathogenic fungal or bacterial species. The Candida albicans enzyme was inhibited with potencies in the range of 3.4-3970 nM, whereas the Mycobacterium tuberculosis enzymes Rv1284 and Rv3273 were inhibited with Kis in the range of 4.8-6500 nM and of 6.4-6850 nM, respectively. The structure-activity relationship for this class of inhibitors is rather complex, but the main features associated with effective inhibition of both α- and β-CAs investigated here have been delineated. The nature of the moiety substituting the second ureido nitrogen is the determining factor in controlling the inhibitory power, probably due to the flexibility of the ureido linker and the possibility of this moiety to orientate in different subpockets of the active site cavities of these enzymes.

Carbonic anhydrase inhibitors - Part 49: Synthesis of substituted ureido and thioureido derivatives of aromatic/heterocyclic sulfonamides with increased affinities for isozyme I

Reaction of nine aromatic/heterocyclic sulfonamides containing a free amino group with aryl isocyanates/isothiocyanates or allyl isothiocyanate afforded the corresponding urea/thiourea derivatives, which were characterized by standard physico-chemical procedures and assayed as inhibitors of three isozymes of carbonic anhydrase (CA), i.e. hCA I, hCA II and bCA IV (h = human, b = bovine isozyme). Another series of compounds, 1,5-disubstituted-2-thiobiuret derivatives, were prepared by reaction of 3,4-dichlorophenyl isocyanate with thioureido-containing aromatic/heterocyclic sulfonamides. Good inhibition of all these three CA isozymes was observed with the new compounds, but an exciting finding was that the ureas/thioureas and especially the above-mentioned thiobiurets reported here have an increased affinity to the slow isozyme hCA I, generally less susceptible to inhibition by sulfonamides, as compared to the rapid isozymes hCA II and bCA IV. Some of the new compounds might constitute good lead molecules for developing more selective CA I inhibitors.