651733-09-4

Upstream product

• 31930-18-4 2-amino-4-nitrobenzamide 
• 619-17-0 4-Nitroanthranilic acid 
• 99-55-8 2-methyl-5-nitroaniline 
• 651733-08-3 2-acetamido-4-nitro-α-phthalimido toluene 

Relevant academic research and scientific papers

Discovery of 5-methyl-N-(2-arylquinazolin-7-yl)isoxazole-4-carboxamide analogues as highly selective FLT3 inhibitors

A series of 4-arylamido 5-methylisoxazole derivatives with quinazoline core was designed and synthesised based on conformational rigidification of a previous type II FMS inhibitor. Most of quinazoline analogues displayed activity against FLT3 and FLT3-ITD. Compound 7d, 5-methyl-N-(2-(3-(4-methylpiperazin-1-yl)-5-(trifluoromethyl)phenyl)quinazolin-7-yl)isoxazole-4-carboxamide, exhibited the most potent inhibitory activity against FLT3 (IC50= 106 nM) with excellent selectivity profiles over 36 other protein kinases including cKit and FMS kinase. Compound 7d was also active in FLT-ITD, with an IC50 value of 301 nM, and other FLT3 mutants showing potential as an AML therapeutics.

HETEROCYCLIDENE-N-(ARYL)ACETAMIDE DERIVATIVE

The blow-described formula (I): [Ch. 1] a compound represented by formula (I) : (wherein k, m, n, and p each represent 0 to 2; j and q represents 0 or 1; R1 represents a halogen atom, a hydrocarbon group, a heterocyclic group, an alkoxy group,

Nitroaryl phosphoramide compositions and methods for targeting and inhibiting undesirable cell growth or proliferation

The present invention relates to nitroaryl-substituted phosphoramide prodrug compounds and methods of producing the same for use in targeting and inhibiting undesirable cell growth or proliferation.

Nitrobenzocyclophosphamides as potential prodrugs for bioreductive activation: Synthesis, stability, enzymatic reduction, and antiproliferative activity in cell culture

In efforts to obtain potential anticancer prodrugs for gene-directed enzyme prodrug therapy using Eschericia coli nitroreductase, a series of four benzocyclophosphamide analogues were designed and synthesized incorporating a strategically placed nitro group in a position para to the benzylic carbon for reductive activation. All four analogues were found to be stable in phosphate buffer at pH 7.4 and 37 °C and were good substrates of E. coli nitroreductase with half lives between 7 and 24 min at pH 7.0 and 37 °C. However, only two analogues 6a and 6c, both with a benzylic oxygen in the phosphorinane ring para to the nitro group, showed a modest 33-36-fold enhanced cytotoxicity in E. coli nitroreductase-expressing cells. These results suggest that good substrate activity and the para benzylic oxygen are required for activation by E. coli nitroreductase. Compounds 6a and 6c represent a new structure type for reductive activation and a lead for further modification in the development of better analogues with improved selective toxicity to be used in gene-directed enzyme prodrug therapy.