251096-79-4

Basic information

• Product Name: 2-[(4-chlorobenzene)sulfonamido]-2-phenylacetic acid
• Synonyms: 2-[(4-chlorobenzene)sulfonamido]-2-phenylacetic acid
• CAS NO: 251096-79-4
• Molecular Formula: C14H12ClNO4S
• Molecular Weight: 325.76738
• Mol File: 251096-79-4.mol
• Article Data: 5

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 2-[(4-chlorobenzene)sulfonamido]-2-phenylacetic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-[(4-chlorobenzene)sulfonamido]-2-phenylacetic acid(251096-79-4)
• EPA Substance Registry System: 2-[(4-chlorobenzene)sulfonamido]-2-phenylacetic acid(251096-79-4)

Safety Data

• Hazardous Substances Data: 251096-79-4(Hazardous Substances Data)

Usage

Purpose

Herbicide for controlling broadleaf weeds and annual grasses in various crops

Physical form

White crystalline solid

Molecular weight

311.76 g/mol

Melting point

187-188°C

Mode of action

Interferes with plant growth and disrupts amino acid synthesis, leading to weed death

Mammalian toxicity

Low

Environmental half-life

Relatively short

Environmental risks

May pose risks to aquatic organisms and non-target plants

Application and handling

Proper procedures should be followed to minimize environmental impact

Upstream product

• 255048-80-7 N-(2,2,2-trichloro-1-phenylethyl)-4-chlorobenzenesulfonamide 
• 875-74-1 (R)-phenylglycine 
• 98-60-2 4-chlorobenzenesulfonyl chloride 
• 2935-35-5 (S)-2-phenylglycine 

Relevant articles and documents

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.

Synthesis of N-(arylsulfonyl)arylglycines and their influence of the growth of bifidobacteria

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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.