80789-74-8

Usage

Air & Water Reactions

Slightly water soluble.

Reactivity Profile

A weak organic base.

Fire Hazard

Flash point data for Sodium 5-sulfoisatin. is not available, but Sodium 5-sulfoisatin. is probably combustible.

InChI:InChI=1/C8H5NO5S.Na/c10-7-5-3-4(15(12,13)14)1-2-6(5)9-8(7)11;/h1-3H,(H,9,10,11)(H,12,13,14);/q;+1/p-1

Upstream product

• 75038-06-1 leuco-indirubin 
• 479-41-4 indirubin 
• 91-56-5 indole-2,3-dione 

Downstream Products

• 1155338-43-4 1-(isatin-5'-sulfonic acid)-4-(4'-methoxyphenyl)-3-thiosemicarbazone 
• 220510-31-6 [2,3-dioxo-5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-2,3-dihydro-indol-1-yl]-acetic acid tert-butyl ester 
• 220509-85-3 5-{[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl}-1H-indole-2,3-dione 
• 220510-17-8 5-(pyrrolidin-1-ylsulfonyl)indoline-2,3-dione 
• 851756-32-6 4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonyl chloride 
• 854948-76-8 acetic acid 2-(8-chlorosulfonyl-1,3-dioxo-4-phenyl-1,3-dihydro-pyrrolo[3,4-c]quinolin-2-yl)-ethyl ester 

Relevant academic research and scientific papers

Phenyl Benzenesulfonylhydrazides Exhibit Selective Indoleamine 2,3-Dioxygenase Inhibition with Potent in Vivo Pharmacodynamic Activity and Antitumor Efficacy

Tryptophan metabolism has been recognized as an important mechanism in immune tolerance. Indoleamine 2,3-dioxygenase plays a key role in local tryptophan metabolism via the kynurenine pathway and has emerged as a therapeutic target for cancer immunotherapy. Our prior study identified phenyl benzenesulfonyl hydrazide 2 as a potent in vitro (though not in vivo) inhibitor of indoleamine 2,3-dioxygenase. Further lead optimization to improve in vitro potencies and pharmacokinetic profiles resulted in N′-(4-bromophenyl)-2-oxo-2,3-dihydro-1H-indole-5-sulfonyl hydrazide 40, which demonstrated 59% oral bioavailability and 73% of tumor growth delay without apparent body weight loss in the murine CT26 syngeneic model, after oral administration of 400 mg/kg. Accordingly, 40, is proposed as a potential drug lead worthy of advanced preclinical evaluation.

Spectroelectrochemistry of solid indirubin and its sulfonated form

Electrochemical processes of solid indirubin and its sulfonated form were comparatively studied in aqueous buffers by cyclic voltammetry and long-path-length thin-layer UV-vis spectroelectrochemistry, using a carbon paste working electrode with or without indirubin particles attached. The two forms of indirubin gave similar voltammetric features as well as main reaction products. Alkaline pH of electrolyte generally had a negative effect on both the reaction systems, compared with the acidic pH. Electro-reduction of both indirubins produced their leuco forms, which can be oxidized back to the initial reactants by oxygen. In the alkaline buffers the leuco-indirubin (not sulfonated) may form aggregates with poor solubility and poor electrochemical reactivity. Electro-oxidation of both indirubins led to the irreversible formation of isatin (sulfonated or not). An EC and ECE mechanisms are proposed for the reduction and the oxidation, respectively, of indirubin in two forms. The combination of solid state and solution phase spectroelectrochemistry shows the advantage of providing multidimensional information for reaction mechanism determination.

5-Pyrrolidinylsulfonyl isatins as a potential tool for the molecular imaging of caspases in apoptosis

Caspases are the unique enzymes responsible for the execution of the cell death program and may represent an exclusive target for the specific molecular imaging of apoptosis in vivo. 5-Pyrrolidinylsulfonyl isatins represent potent nonpeptidyl caspase inhibitors that may be suitable for the development of caspase binding radioligands (CBRs). (S)-5-[1-(2-Methoxymethylpyrrolidinyl) sulfonyl]isatin (7) served as a lead compound for modification of its N-1-position. Corresponding pairs of N-1-substituted 2-methoxymethyl- and 2-phenoxymethylpyrrolidinyl derivatives were examined in vitro by biochemical caspase inhibition assays. All target compounds possess high in vitro caspase inhibition potencies in the nanomolar to subnanomolar range for caspase-3 (Ki = 0.2-56.1 nM). As shown for compound (S)-1-(4-(2-fluoroethoxy) benzyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin (35), the class of N-1-substituted 5-pyrrolidinylsulfonyl isatins competitively inhibits caspase-3. All caspase inhibitors show selectivity for the effector caspases-3 and -7 in vitro. The 2-methoxymethylpyrrolidinyl versions of the isatins appear to possess superior caspase inhibition potencies in cellular apoptosis inhibition assays compared with the 2-phenoxymethylpyrrolidinyl inhibitors.