3523-95-3

Usage

Chemical structure

1,3,4-Thiadiazole-2-sulfonamide, 5-(((4-aminophenyl)sulfonyl)amino)-
The compound has a thiadiazole ring fused with a sulfonamide group and an aminophenylsulfonyl group attached to the thiadiazole ring.

Sulfonamide derivative

It is a derivative of sulfonamide, a class of compounds known for their antimicrobial properties.

Potential antineoplastic activity

The compound has been studied for its potential use in cancer treatment, as it may help inhibit the growth of cancer cells.

Potential antimicrobial activity

It has been investigated for its ability to inhibit the growth of certain microorganisms, making it a potential candidate for antimicrobial applications.

Mechanism of action

Interference with folic acid synthesis
The compound works by disrupting the synthesis of folic acid, which is crucial for the growth of cancer cells and the survival of certain bacteria.

Ongoing research

Further studies are being conducted to explore the potential therapeutic applications of 1,3,4-Thiadiazole-2-sulfonamide, 5-(((4-aminophenyl)sulfonyl)amino)- in various medical fields.

InChI:InChI=1/C8H9N5O4S3/c9-5-1-3-6(4-2-5)20(16,17)13-7-11-12-8(18-7)19(10,14)15/h1-4H,9H2,(H,11,13)(H2,10,14,15)

Upstream product

• 3523-96-4 N-(4-(N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)sulfamoyl)phenyl)acetamide 
• 121-60-8 p-acetylaminobenzenesulfonyl chloride 

Downstream Products

• 729-46-4 4,4'-(dithiodicarbonothioyl)dimorpholine 
• 137-26-8 Thiram 

Relevant academic research and scientific papers

Development of sulfonamide AKT PH domain inhibitors

Disruption of the phosphatidylinositol 3-kinase/AKT signaling pathway can lead to apoptosis in cancer cells. Previously we identified a lead sulfonamide that selectively bound to the pleckstrin homology (PH) domain of AKT and induced apoptosis when present at low micromolar concentrations. To examine the effects of structural modification, a set of sulfonamides related to the lead compound was designed, synthesized, and tested for binding to the expressed PH domain of AKT using a surface plasmon resonance-based competitive binding assay. Cellular activity was determined by means of an assay for pAKT production and a cell killing assay using BxPC-3 cells. The most active compounds in the set are lipophilic and possess an aliphatic chain of the proper length. Results were interpreted with the aid of computational modeling. This paper represents the first structure-activity relationship (SAR) study of a large family of AKT PH domain inhibitors. Information obtained will be used in the design of the next generation of inhibitors of AKT PH domain function.

SMALL MOLECULE INHIBITORS OF THE PLECKSTRIN HOMOLOGY DOMAIN AND METHODS FOR USING SAME

Pleckstrin homology domain binding compounds, pharmaceutical compositions including such compounds, and methods for their use are described herein.

Carbonic anhydrase inhibitors. Inhibition of tumor-associated isozyme IX by halogenosulfanilamide and halogenophenylaminobenzolamide derivatives

Two series of halogenated sulfonamides have been prepared. The first consists of mono/ dihalogenated sulfanilamides, whereas the second one consists of the mono/dihalogenated aminobenzolamides, incorporating equal or different halogens (F, Cl, Br, and I). These sulfonamides have been synthesized from the corresponding anilines by acetylation (protection of the amino group), chlorosulfonylation, followed either by amidation, or reaction with 5-amino1,3,4-thiadiazole-2-sulfonamide (and eventually deacetylation). All these compounds, together with the six clinically used sulfonamide inhibitors (acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, and brinzolamide) were investigated as inhibitors of the transmembrane, tumor-associated isozyme carbonic anhydrase (CA) IX. Inhibition data against the classical, physiologically relevant isozymes I, II, and IV were also obtained. CA IX shows an inhibition profile which is generally completely different from those of isozymes I, II, and IV, with potent inhibitors (inhibition constants in the range of 12-40 nM) among both simple aromatic (such as 3-fluoro-5-chloro-4-aminobenzenesulfonamide) as well as heterocyclic compounds (such as acetazolamide, methazolamide, 5-amino-1,3,4-thiadiazole-2-sulfonamide, aminobenzolamide, and dihalogenated aminobenzolamides). This first detailed CA IX inhibition study revealed many interesting leads, suggesting the possibility to design even more potent and eventually CA IX-selective inhibitors, with putative applications as antitumor agents.

Carbonic anhydrase inhibitors - Part 29: Interaction of isozymes I, II and IV with benzolamide-like derivatives

Reaction of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-imino-4- methyl-2-sulfonamido-δ2-1,3,4-thiadiazoline with sulfonyl halides/sulfonic acid anhydrides afforded benzolamide-like derivatives possessing strong inhibitory effects towards three isozymes of carbonic anhydrase (CA), CA I, II anal IV. Some of the compounds were designed in such a way to possess good leaving groups (such as nitro-; 2,4,6-triphenyl-pyridinium, etc.) for aromatic nucleophilic substitution reactions with fluoride, in order to introdUCe positron-emitting isotopes in their molecule, such as 18F. Reactions done initially with the stable isotope of fluorine were not very effective, as the yields in the desired fluoro-derivatives were low, and a complex reaction mixture was obtained. By using this type of approach, and optimizing the synthetic procedure, CA inhibitors for positron emission tomography (PET) applications might be obtained (in the case utilizing a carrier, which is the non-radioactive derivative itself, since the affinities of such derivatives for the receptor are in the nanomolar range). Further improving of such synthetic procedures might lead to better yields and the respective CompOUnds should be used as selective ligands (also in carrier- free systems) in assessing the role of membrane bound CA isozymes or for new diagnostic tools based on PET.

Renal and cerebrospinal fluid formation pharmacology of a high molecular weight carbonic anhydrase inhibitor

To achieve selective inhibition of cytosolic and membrane-bound carbonic anhydrase (CA II and CA IV, respectively), we synthesized a polymer of molecular weight 3500 from polyoxyethylene bis acetic acid and aminobenzolamide. The new compound, designated F

Synthesis and properties of two new membrane-impermeant high-molecular-weight carbonic anhydrase inhibitors

The synthesis and inhibitory properties and stability of two nontoxic high-molecular-weight carbonic anhydrase inhibitors (F 3500 and POBUMS) are reported. F 3500 was prepared by the covalent linkage of aminobenzolamide, a potent carbonic anhydrase (CA) inhibitor, to polyoxyethylene bisacetic acid (MW 3350). Linkage of the same inhibitor to polybutadiene maleic acid copolymer (MW 20,000) gave POBUMS. They contained on a mole percentage basis 0.11-0.28% unreacted aminobenzolamide as contaminant. F 3500 and POBUMS were approximately equipotent as carbonic anhydrase inhibitors on a weight basis with K(i) at 37°C for CA II and CA IV of approximately 0.5 and 10 μg/ml, respectively. They showed a maximum release of 28% aminobenzolamide when heated at 70°C for 3 days at pH 10.5 and were completely stable toward enzymatic hydrolysis (protease and peptidase at 25°C). They were not membrane permeable as judged by their inability to bind to intracellular CA II in intact red cells, nor were they actively uptaken in rat kidney slices. Rats injected with F 3500 (200 mg/kg) showed no toxicity and excreted 93% of the polymer unchanged in the urine in 3 h. The two polymers should prove useful for in vivo and in vitro studies of selective CA IV inhibition in membranes.