617-10-7

Usage

InChI:InChI=1/C9H8N2O5/c12-8(13)5-10-9(14)6-2-1-3-7(4-6)11(15)16/h1-4H,5H2,(H,10,14)(H,12,13)/p-1

Upstream product

• 495-69-2 Hippuric Acid 
• 60247-35-0 N-(3-nitro-benzoyl)-glycine ethyl ester 
• 56-40-6 glycine 
• 121-90-4 m-nitrobenzoic acid chloride 
• 75152-22-6 2-(3-Nitro-phenyl)-4H-oxazol-5-one 
• 121-92-6 3-nitrobenzoic acid 

Downstream Products

• 60247-35-0 N-(3-nitro-benzoyl)-glycine ethyl ester 
• 20938-64-1 N-(3-Aminobenzoyl)glycine 
• 4211-96-5 2-(3-nitro-phenyl)-4-thiophen-2-ylmethylene-4H-oxazol-5-one 
• 22269-65-4 4-(4-dimethylamino-2-methyl-benzylidene)-2-(3-nitro-phenyl)-4H-oxazol-5-one 
• 19646-41-4 3,3'-{4-[2-(3-nitro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-phenylazanediyl}-bis-propionitrile 
• 20448-30-0 3,3'-{3-methyl-4-[2-(3-nitro-phenyl)-5-oxo-oxazol-4-ylidenemethyl]-phenylazanediyl}-bis-propionitrile 
• 39052-68-1 4-[4-(benzyl-methyl-amino)-benzylidene]-2-(3-nitro-phenyl)-4H-oxazol-5-one 
• 75152-12-4 (3-Nitro-benzoylamino)-acetic acid 4-nitro-phenyl ester 
• 75152-22-6 2-(3-Nitro-phenyl)-4H-oxazol-5-one 
• 525580-11-4 N-(2-hydrazinyl-2-oxoethyl)-3-nitrobenzamide 
• 861568-35-6 N-(3-nitro-benzoyl)-glycyl azide 

Relevant academic research and scientific papers

Exploration of secondary and tertiary pharmacophores in unsymmetrical N,N′-diaryl urea inhibitors of soluble epoxide hydrolase

The impact of various secondary and tertiary pharmacophores on in vitro potency of soluble epoxide hydrolase (sEH) inhibitors based on the unsymmetrical urea scaffold 1 is discussed. N,N′-Diaryl urea inhibitors of soluble epoxide hydrolase exhibit subtle variations in inhibitory potency depending on the secondary pharmacophore but tolerate considerable structural variation in the second linker/tertiary pharmacophore fragment.

Novel synthesis and characterization of some new-2-(R) phenyl- 4-(-4-bromo-2-fluoro benzylidene)-oxazol-5-ones

In the present study a series of some new 2-(substituted) phenyl- 4-(4-bromo-2-fluoro benz-ylidene)-oxazol-5-ones (2a-2j) were synthesized by the condensation of selected substituted benzoyl glycine (1a-1j) with 4-bromo-2-fluoro benzaldehyde in the presence of fused sodium acetate and acetic anhydride. The constitution of the newly synthesized compounds has been supported by their physical properties, elemental analysis, colour, m.p, IR spectral analysis data.

A facile synthesis of N-formylbenzamides by oxidative decarboxylation of N-aroylglycine induced by Ag+/S2O82-

A facile method is described for the synthesis of N-formylbenzamides by oxidative decarboxylation of N-aroylglycine using catalytic silver(I) and 2 equivalents of ammonium persulfate as an oxidant in a biphasic system (CHCl 3/water).

META-GUANIDINE, UREA, THIOUREA OR AZACYCLIC AMINO BENZOIC ACID DERIVATIVES AS INTEGRIN ANTAGONISTS

The present invention relates to a class of compounds represented by the Formula Ior a pharmaceutically acceptable salt thereof, whereinA ispharmaceutical compositions thereof and methods of using such compounds and compositions as alphavbeta3 antagonists.

Relative Structure-Inhibition Analyses of the N-Benzoyl and N-(Phenylsulfonyl) Amino Acid Aldose Reductase Inhibitors

A number of N-benzoyl amino acids were synthesized and tested to compare structure-inhibition relationships with the isosteric N-(phenylsulfonyl) amino acid (PS-amino acid) aldose reductase inhibitors.Inhibition analyses with these series reveals that their kinetic mechanisms of inhibition are similar, but that significant differences in structure-inhibition relationships exist.For example, while the PS-alanines and PS-2-phenylglycines produce enantioselective inhibition (S > R), no consistent pattern of enantioselectivity is observed with the isosteric N-benzoylalanines and 2-phenylglycines.Also, N-methyl and N-phenyl substitution in the PS-amino acid series does not substantially alter inhibitory activity, while similar substitutions in the N-benzoyl series (particularly N-phenyl) results in a significant increase in inhibitory activity.Proton NMR analysis of the N-benzoylsarcosines reveals that these compounds exist as a mixture of rotamers in solutions including the enzyme assay buffer and that the preferred conformer is one in which the carboxymethyl moiety is trans to the aromatic ring.Similar analyses with the N-benzoyl-N-phenylglycines demonstrate that these derivatives exist exclusively in the trans rotameric conformation in solution.No such N-substituent effects on conformation were observed in the PS-amino acid series.These results suggest that the differences in structure-inhibition trends between these structurally related series may result from the effect of substituents on preferred conformation.

Synthesis and in Vitro Aldolase Reductase Inhibitory Activity of Compounds Containing an N-Acylglycine Moiety

A number of N-benzoylglycines (6), N-acetyl-N-phenylglycines (7), N-benzoyl-N-phenylglycines (8), and tricyclic N-acetic acids (9-12) were synthesized as analogues of the N-acylglycine-containing aldolase reductase inhibitors alrestatin and 2-oxoquinoline-1-acetic acid.Derivatives of 6, which represent ring-simplified analogues of alrestatin, are very weak inhibitors of aldolase reductase obtained from rat lens, producing 50percent inhibition only at concentrations exceeding 100 μM.Compounds of series 7 were designed as ring-opened analogues of the 2-oxoquinolines.While this derivatives are more potent than compounds of series 6 (IC 50s of 6-80 μM), they are less active than the corresponding 2-oxoquinolines.Analogues of series 8 were designed as hybrid structures of both alrestatin and the 2-oxoquinoline-1-acetic acids.These compounds are substantially more potent than compounds of series 6 and 7 and display inhibitory activities comparable to or greater than alrestatin or the 2-oxoquinolines (IC 50s of 0.1-10 μM).Of the rigid analogues of 8, the most potent derivative is benzoxindol (12) with an IC 50 of 0.67 μM, suggesting that fusion of the two aromatic rings of 8 in a coplanar conformation may optimize affinity for aldose reductase in this series.

Structure-Reactivity Studies on the Equilibrium Reaction between Phenolate Ions and 2-Aryloxazolin-5-ones: Data Consistent with a Concerted Acyl-Group-Transfer Mechanism

The rate and equilibrium constants for the reaction between phenolate anions and 2-aryloxazolin-5-ones have been measured as a function of the structures Ar and Ar'.The change in "effective" charge on both phenol-leaving oxygen and endocyclic oxygen from ground to transition state, as determined from the relevant Broensted parameters, is substantial and essentially additive consistent with a concerted displacement mechanism.The stepwise mechanism requires a small change in effective charge on the phenol oxygen because departure of phenolate ion from the tetrahedral intermediate cannot be rate limiting.Hydroxide ion attack on the C-5 atom of the oxazolinone to yield a benzoylglycine has a Hammett ?- dependence which can only arise from a concerted displacement; the rate-limiting step for the stepwise mechanism is the addition of hydroxide and the transition state of the rate-limiting step will therefore not involve much endocyclic C-O bond fission.An inverse deuterium oxide solvent isotope effect indicates that the observed general-acid catalysis has a specific-acid/nucleophilic mechanism; both hydroxide and oxonium ion catalysis are demonstrated by using 18O-labeling experiments to involve nucleophilic attack at the carbonyl (C-5) center.The equilibrium constant for reaction of azide ion with 2-phenyloxazolin-5-ones has been measured; it is suggested that the absence of racemization during azide coupling in peptide synthesis is related to the very unfavorable equilibrium constant for oxazolinone formation compared with that of activated oxygen esters.