13029-74-8

Usage

Uses

Used in Pain Management:
[(4-METHOXYPHENYL)SULFONYL]AMINOACETIC ACID is used as an analgesic for the management of moderate-to-severe pain, particularly menstrual pain. It is effective in reducing inflammation and alleviating pain by inhibiting the production of prostaglandins, which are responsible for pain and inflammation.
Used in Inflammation Reduction:
In the medical industry, [(4-METHOXYPHENYL)SULFONYL]AMINOACETIC ACID is used as an anti-inflammatory agent to reduce inflammation caused by various conditions, such as arthritis, muscle strains, and other inflammatory disorders. Its ability to inhibit cyclooxygenase enzyme activity helps in decreasing the production of prostaglandins, thereby reducing inflammation.
Used in Gastrointestinal Protection:
When taken with food or milk, [(4-METHOXYPHENYL)SULFONYL]AMINOACETIC ACID can be used to minimize the risk of stomach irritation, which is a common side effect of NSAIDs. This practice helps in protecting the gastrointestinal tract from potential damage caused by the medication.
Precautions:
[(4-METHOXYPHENYL)SULFONYL]AMINOACETIC ACID should be used with caution in individuals with a history of heart disease, high blood pressure, or stomach ulcers, as it may exacerbate these conditions or cause additional side effects. Common side effects of Mefenamic acid include stomach upset, nausea, vomiting, diarrhea, and dizziness. It is essential to follow the prescribed dosage and consult a healthcare professional for any concerns or questions regarding its use.

InChI:InChI=1/C9H11NO5S/c1-15-7-2-4-8(5-3-7)16(13,14)10-6-9(11)12/h2-5,10H,6H2,1H3,(H,11,12)/p-1

Upstream product

• 1129-26-6 4-methoxybenzene sulfonamide 
• 3926-62-3 sodium monochloroacetic acid 
• 86674-19-3 C₉H₁₀N₂O₇S 
• 98-68-0 4-methoxy-phenyl-sulphonyl chloride 
• 56-40-6 glycine 
• 154853-46-0 2,4-dinitrophenyl 4-methoxybenzenesulfonate 
• 1388830-18-9 C₂₈H₃₅N₃O₉S 

Downstream Products

• 83800-71-9 1-(4-Methoxy-benzenesulfonyl)-2-thioxo-imidazolidin-4-one 
• 1027833-26-6 C₁₄H₁₉NO₇S 
• 83800-79-7 1-(4-Methoxy-benzenesulfonyl)-imidazolidine-2,4-dione 

Relevant academic research and scientific papers

Deconstructing Noncovalent Kelch-like ECH-Associated Protein 1 (Keap1) Inhibitors into Fragments to Reconstruct New Potent Compounds

Targeting the protein-protein interaction (PPI) between nuclear factor erythroid 2-related factor 2 (Nrf2) and Kelch-like ECH-associated protein 1 (Keap1) is a potential therapeutic strategy to control diseases involving oxidative stress. Here, six classes of known small-molecule Keap1-Nrf2 PPI inhibitors were dissected into 77 fragments in a fragment-based deconstruction reconstruction (FBDR) study and tested in four orthogonal assays. This gave 17 fragment hits of which six were shown by X-ray crystallography to bind in the Keap1 Kelch binding pocket. Two hits were merged into compound 8 with a 220-380-fold stronger affinity (Ki = 16 μM) relative to the parent fragments. Systematic optimization resulted in several novel analogues with Ki values of 0.04-0.5 μM, binding modes determined by X-ray crystallography, and enhanced microsomal stability. This demonstrates how FBDR can be used to find new fragment hits, elucidate important ligand-protein interactions, and identify new potent inhibitors of the Keap1-Nrf2 PPI.

Development of Piperazinediones as dual inhibitor for treatment of Alzheimer's disease

Novel multifunctional 3,6-Diphenyl-1,4-bis(phenylsulfonyl)piperazine-2,5-dione derivatives were designed and synthesized for the treatment of Alzheimer's disease (AD). The designed scaffold has blood brain barrier penetrating ability, acetylcholinesterase (AChE) and matrix metalloproteinase-2 (MMP-2) inhibition potential. Compounds 52 and 46 showed very significant inhibition against AChE, IC50 = 32.45 ± 0.044, 28.65 ± 0.029, BuChE, IC50 = 157.95 ± 0.264, 160.58 ± 0.082 and MMP-2, IC50 = 36.83 ± 0.015, 19.57 ± 0.005 (nM). In the enzyme kinetics study, lead molecule 46 showed non-competitive inhibition of AChE with Ki = 7 nM and competitive inhibition of MMP-2 with Ki = 20 nM. Compounds 52 and 46 inhibited AChE-induced Aβ aggregation at 20 μM. The compounds also exhibited in-vitro antioxidant potential in DPPH assay. Further, compound 46 was found to be a promising neuroprotective agent in MC65 cells. Lead molecule 46 significantly enhanced working memory in scopolamine induced amnesia animal model at dose of 5 mg/kg dose. The mitochondrial membrane potential was restored in animals when treated with compounds 52 and 46.

Design, synthesis and in vitro evaluation studies of sulfonyl-amino-acetamides as small molecule BACE-1 inhibitors

The identification of a series of sulfonyl-amino-acetamides as BACE-1 (β-secretase) inhibitors for the treatment of Alzheimer's disease is reported. The derivatives were designed based on the docking simulation study, synthesized and assessed for BACE-1 inhibition in vitro. The designed ligands revealed desired binding interactions with the catalytic aspartate dyad and occupance of S1 and S2′ active site regions. These in silico results correlated well with in vitro activity. Out of 33 compounds synthesized, 12 compounds showed significant inhibition at 10 μM concentration. The most active compound 2.17S had IC50 of 7.90 μM against BACE-1, which was concomitant with results of in silico docking study.

Target-activated prodrugs (TAPs) for the autoregulated inhibition of MMP12

We describe a prodrug concept in which the target enzyme MMP12 produces its own inhibitor in a two-step activation procedure. By using an MMP12-specific peptide sequence and a known sulfonamide drug integrated in the backbone, the active inhibitor is released upon enzyme cleavage. In in vitro experiments, we present proof of concept that the activation proceeds with useful kinetics. The approach is highly selective over the closely related MMP8. If applied in vivo in the future, these prodrugs might release the active entity in a highly specific manner only at such sites where enzyme activity resides.

Design and synthesis of procollagen C-proteinase inhibitors

Non-peptidic inhibitors of procollagen C-proteinase (PCP) were designed from substrate leads. Compounds were optimized for potency and selectivity, with N-substituted aryl sulfonamide hydroxamates having the best combination of these properties. Compounds

Effect of substituent on regioselectivity and reaction mechanism in aminolysis of 2,4-dinitrophenyl X-substituted benzenesulfonates

(Chemical Equation Presented) We report on a kinetic study for the nucleophilic substitution reactions of 2,4-dinitrophenyl X-substituted benzensulfonates (X = 4-MeO, 1a, and X = 4-NO2, 1c) with a series of primary amines in 80 mol % H2O/20 mol % DMSO at 25.0 °C. The reactions proceed through S-O and C-O bond fission pathways competitively. The fraction of the S-O bond fission increases as the attaching amine becomes more basic and the substituent X changes from 4-MeO to 4-NO2, indicating that the regioselectivity is governed by the electronic nature of the substituent X as well as the basicity of amines. The S-O bond fission has been suggested to proceed through an addition intermediate with a change in the rate-determining step (RDS) at pK°a = 8.9 ± 0.1. The electronic nature of the substituent X influences kNS-O and k1 values, but not the k2/k-1 ratios and the pK°a value significantly. Stabilization of the ground state (GS) through resonance interaction between the electron-donating substituent and the electrophilic center has been suggested to be responsible for the decreased reactivity of 1a compared to 1c. The second-order rate constants for the C-O bond fission exhibit no correlation with the electronic nature of the substituent X. The distance effect and the nature of the reaction mechanism have been suggested to be responsible for the absence of the correlation.

2,3,4,5-tetrahydro-1H-(1,4)benzodiazepine-3-hydroxamic acids

Compounds having the following formula: ? are useful in treating disease conditions mediated by matrix metalloproteinases and TACE, such as tumor growth, osteoarthritis, rheumatoid arthritis and degenerative cartilage loss.

2,3,4,5-tetrahydro-1H-[1,4]-benzodiazepine-3-hydroxyamic acids

Compounds are provided having the following formula: wherein R, R1, R2, R3, and R4 are defined in the specification, which have matrix metalloproteinase inhibiting activity.

Protease inhibitors - Part 5. Alkyl/arylsulfonyl- and arylsulfonylureido-/arylureido- glycine hydroxamate inhibitors of Clostridium histolyticum collagenase

Reaction of alkyl/arylsulfonyl halides with glycine afforded a series of derivatives which were first N-benzylated by treatment with benzyl chloride, and then converted to the corresponding hydroxamic acids with hydroxylamine in the presence of carbodiimide derivatives. Other derivatives were obtained by reaction of N-benzyl-glycine with aryl isocyanates, arylsulfonyl isocyanates or benzoyl isothiocyanate, followed by conversion of their COOH group into the CONHOH moiety, as mentioned above. The 90 new compounds reported here were assayed as inhibitors of the Clostridium histolyticum collagenase (EC 3.4.24.3), a zinc enzyme which degrades triple helical regions of native collagen. The prepared hydroxamate derivatives were generally 100-500 times more active than the corresponding carboxylates. In the series of synthesized hydroxamates, substitution patterns leading to the best inhibitors were those involving perfluoroalkylsulfonyl- and substituted- arylsulfonyl moieties, such as pentafluorophenylsulfonyl, 3- and 4- carboxyphenylsulfonyl-, 3-trifluoromethyl-phenylsulfonyl or 1- and 2-naphthyl among others. Thus, it seems that similarly to the matrix metalloproteinase (MMP) hydroxamate inhibitors, Clostridium histolyticum collagenase inhibitors should incorporate hydrophobic moieties at the P1, and P2, sites, whereas the α-carbon substituent may be a small and compact moiety (such as H. for the Gly derivatives reported here). Such compounds might lead to the design of collagenase inhibitor-based drugs useful as anti-cancer, anti-arthritis or anti-bacterial agents for the treatment of corneal keratitis. (C) 2000 Editions scientifiques et medicales Elsevier SAS.

Carbonic anhydrase and matrix metalloproteinase inhibitors: Sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes

The 14 different carbonic anhydrase (CA, EC 4.2.1.1) isozymes as well as the 23 different matrix metalloproteinases (MMPs) isolated up to now in higher vertebrates play important physiological functions in these organisms. Unsubstituted sulfonamides act a