96686-12-3

Upstream product

• 875-74-1 (R)-phenylglycine 
• 98-68-0 4-methoxy-phenyl-sulphonyl chloride 
• 206758-53-4 2(R)-[(4-methoxybenzenesulfonyl)amino]-2-phenyl acetic acid methyl ester 

Downstream Products

• 206758-46-5 N-hydroxy-2(R)-[(4-methoxybenzenesulfonyl)amino]-2-phenyl acetamide 
• 1027473-92-2 (R)-2-[Benzyl-(4-methoxy-benzenesulfonyl)-amino]-N-tert-butoxy-2-phenyl-acetamide 
• 1025880-05-0 (R)-[Benzyl-(4-methoxy-benzenesulfonyl)-amino]-phenyl-acetic acid tert-butyl ester 
• 1026359-29-4 (R)-[Benzyl-(4-methoxy-benzenesulfonyl)-amino]-phenyl-acetic acid 

Relevant academic research and scientific papers

ALPHA-AMINO SULFONYL HYDROXAMIC ACIDS AS MATRIX METALLOPROTEINASE INHIBITORS

A compound of formula I or pharmaceutical acceptable salts thereof, I wherein R1 is isopropyl, 2-methylbut-2yl, phenyl, benzyl, or 1H-indol-3ylmethyl; R2 is n-octyl, phenyl, or phenyl substituted with methoxy, fluoro, or bromo, are matrix metallop

ALPHA-AMINO SULFONYL HYDROXAMIC ACIDS AS MATRIX METALLOPROTEINASE INHIBITORS

A compound of formula I or pharmaceutical acceptable salts thereof, STR1 wherein R 1 is isopropyl, 2-methylbut-2yl, phenyl, benzyl, or 1H-indol-3ylmethyl; R 2 is n-octyl, phenyl, or phenyl substituted with methoxy, fluoro, or bromo, are matrix metalloproteinase inhibitors.

Discovery of CGS 27023A, a non, peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits

Structure-activity relationships of a lead hydroxamic acid inhibitor of recombinant human stromelysin were systematically defined by taking advantage of a concise synthesis that allowed diverse functionality to be explored at each position in a template. An ex vivo rat model and an in vivo rabbit model of stromelysin-induced cartilage degradation were used to further optimize these analogs for oral activity and duration of action. The culmination of these modifications resulted in CGS 27023A, a potent, orally active stromelysin inhibitor that blocks the erosion of cartilage matrix.

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.