117309-47-4

Usage

Uses

Used in Pharmaceutical Industry:
2-([(4-CHLOROPHENYL)SULFONYL]AMINO)-2-PHENYLACETIC ACID is used as a non-steroidal anti-inflammatory drug (NSAID) for its ability to reduce pain and inflammation associated with conditions like arthritis. Its mechanism of action involves the inhibition of prostaglandin production, thereby alleviating the symptoms of these conditions.
Used in Pain Management:
2-([(4-CHLOROPHENYL)SULFONYL]AMINO)-2-PHENYLACETIC ACID serves as an analgesic, providing relief from various types of pain. Its effectiveness in pain management makes it a valuable asset in the treatment of acute and chronic pain conditions.
Used in Inflammation Reduction:
2-([(4-CHLOROPHENYL)SULFONYL]AMINO)-2-PHENYLACETIC ACID is utilized for its anti-inflammatory capabilities, helping to decrease inflammation in the body, which is crucial for the management of inflammatory diseases.
Used in Cancer Research:
Although not yet a standard application, 2-([(4-CHLOROPHENYL)SULFONYL]AMINO)-2-PHENYLACETIC ACID is being studied for its potential use in the treatment of certain types of cancer. The exploration of its anti-cancer properties is an emerging area of research, indicating possible future applications in oncology.

InChI:InChI=1/C14H12ClNO4S/c15-11-6-8-12(9-7-11)21(19,20)16-13(14(17)18)10-4-2-1-3-5-10/h1-9,13,16H,(H,17,18)/p-1/t13-/m1/s1

Upstream product

• 2935-35-5 (S)-2-phenylglycine 
• 98-60-2 4-chlorobenzenesulfonyl chloride 

Downstream Products

• 635291-25-7 4-Chloro-N-[(1S)-2-hydroxy-1-phenylethyl]benzenesulfonamide 

Relevant academic research and scientific papers

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.

Discovery of a novel series of Notch-sparing γ-secretase inhibitors

Using a cell-based assay, we have identified a new series of Notch-sparing γ-secretase inhibitors from HTS screening leads 2a and 2e. Lead optimization studies led to the discovery of analog 8e with improved γ-secretase inhibitory potency and Notch-sparing selectivity.

N- and 2-Substituted N-(Phenylsulfonyl)glycines as Inhibitors of Rat Lens Aldose Reductase

A variety of N-(phenylsulfonyl)-N-phenylglycines 5, N-(phenylsulfonyl)-2-phenylglycines 6, and N-(phenylsulfonyl)anthranilic acids 7 were prepared as analogues of the N-(phenylsulfonyl)glycine 1 aldose reductase inhibitors.In the rat lens assay, several derivatives of 5 display greater inhibitory activity than the corresponding glycines 1, suggesting that N-phenyl substitution enhances affinity for aldose reductase.Enzyme kinetic evaluations of the 4-benzoylamino analogues of 5 and 1 demonstrate that these compounds produce inhibition by the same mechanism.However, the significant differences in relative inhibitory potencies between compounds of series 5 and 1 may indicate that these compounds do not interact with the inhibitor binding site in precisely the same manner.Evaluation of the individual enantiomers of series 6 reveals that the S isomers are substantially more active than the corresponding R isomers.Also, with the exception of the naphthalene analogue 6n, the S stereoisomers of this series display greater inhibitory potencies than the glycines 1.The anthranilates 7 generally are less active than the glycines 1, demonstrating that direct incorporation of an aromatic ring in the glycine side chain may result in a decrease in affinity for aldose reductase.