80866-88-2

Usage

Uses

Used in Pharmaceutical Synthesis:
3-Methoxy-4-nitrobenzyl alcohol is used as a key intermediate in the synthesis of various pharmaceutical compounds. Its unique structure allows for the formation of new aryl azides, such as 3-methoxy-4-nitrobenzyl azide, which can be further utilized in the development of potential photoaffinity labeling reagents for tubulin.
Used in Chemical Research:
In the field of chemical research, 3-Methoxy-4-nitrobenzyl alcohol is used as a starting material for the synthesis of various organic compounds. For example, it can be oxidized to form 3-methoxy-4-nitrobenzaldehyde, which can be further used in the synthesis of other organic compounds.
Used in the Synthesis of Trifluoromethyl-Substituted Hydantoins:
3-Methoxy-4-nitrobenzyl alcohol is used as a precursor in the synthesis of 4-[3-(2-methylphenyl)ureido]-3-methoxybenzylchloride, which is an essential compound required for the synthesis of trifluoromethyl-substituted hydantoins. These hydantoins have potential applications in various fields, including pharmaceuticals and materials science.

InChI:InChI=1/C8H9NO4/c1-13-8-4-6(5-10)2-3-7(8)9(11)12/h2-4,10H,5H2,1H3

Upstream product

• 5081-37-8 methyl 3-methoxy-4-nitrobenzoate 
• 5081-36-7 3-methoxy-4-nitrobenzoic acid 
• 80410-57-7 3-methoxy-4-nitrobenzaldehyde 

Downstream Products

• 68837-96-7 4-(chloromethyl)-2-methoxy-1-nitrobenzene 
• 23145-65-5 1-bromomethyl-3-methoxy-4-nitrobenzene 
• 457099-55-7 4-Benzyloxymethyl-2-methoxy-1-nitro-benzene 
• 103-50-4 dibenzyl ether 
• 306769-04-0 4-[3-(2-methylphenyl)ureido]-3-methoxybenzyl alcohol 
• 457099-58-0 N-benzyl-N-(3-methoxy-4-nitro-benzyl)-amine 
• 457099-59-1 benzyl-(3-methoxy-4-nitro-benzyl)-carbamic acid tert-butyl ester 
• 1349744-63-3 (4-amino-3-methoxy-benzyl)-benzyl-carbamic acid tert-butyl ester 
• 1349744-64-4 benzyl-{4-[3-(5-cyano-pyrazin-2-yl)-ureido]-3-methoxy-benzyl}-carbamic acid tert-butyl ester 
• 1349743-19-6 1-[4-(benzylamino-methyl)-2-methoxy-phenyl]-3-(5-cyano-pyrazin-2-yl)-urea 
• 1612184-59-4 C₂₃H₂₃N₃O₄ 
• 1612184-60-7 C₃₅H₃₈N₄O₆ 
• 1612184-51-6 (E)-2-(2-(4-amino-3-methoxystyryl)-6-methyl-4H-pyran-4-ylidene)malononitrile 
• 1612184-49-2 (E)-2-(2-(4-(4-aminobenzylamino)-3-methoxystyryl)-6-methyl-4H-pyran-4-ylidene)malononitrile 

Relevant academic research and scientific papers

Diphenyl-aminopyrimidine compound for inhibiting kinase activity

The invention relates to a diphenyl-aminopyrimidine compound with an inhibiting function on protein tyrosine kinase, a pharmaceutical composition containing the diphenyl-aminopyrimidine compound, andpreparation and application of the diphenyl-aminopyrimidine compound, in particular to a compound shown as the formula (I) and pharmaceutically acceptable salt or crystal forms or prodrugs or metabolin or aquo-complex or solvate or isotope derivatives thereof, wherein R1, R2, R5, R6, R7, R8 and W are defined as the description. The compound can be used for treating ALK-mediated cancer related symptoms, such as non-small cell lung cancer or breast cancer or neural tumors or esophagus cancer or soft tissue cancer or lymphoma or leukemia. The formula is shown in the specification.

Affinity-Driven Covalent Modulator of the Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Cascade

Traditional medicines provide a fertile ground to explore potent lead compounds, yet their transformation into modern drugs is fraught with challenges in deciphering the target that is mechanistically valid for its biological activity. Herein we reveal that (Z)-(+)-isochaihulactone (1) exhibited significant inhibition against multiple-drug-resistant (MDR) cancer cell lines and mice xenografts. NMR spectroscopy showed that 1 resisted an off-target thiolate, thus indicating that 1 was a target covalent inhibitor (TCI). By identifying the pharmacophore of 1 (α,β-unsaturated moiety), a probe derived from 1 was designed and synthesized for TCI-oriented activity-based proteome profiling. By MS/MS and computer-guided molecular biology approaches, an affinity-driven Michael addition of the noncatalytic C247 residue of GAPDH was found to control the “ON/OFF” switch of apoptosis through non-canonically nuclear GAPDH translocation, which bypasses the common apoptosis-resistant route of MDR cancers.

BICYCLIC INHIBITORS OF ALK

The present invention relates to compounds of formula (1) or pharmaceutical acceptable salts, Formula (1) wherein R1, R2, R3, X, Y, Z, A, B, G1, m, and n are defined in the description. The present invention relates also to compositions containing said compounds which are useful for inhibiting kinases such as ALK and methods of treating diseases such as cancer.

BICYCLIC INHIBITORS OF ALK

The present invention relates to compounds of formula (1) or pharmaceutical acceptable salts, Formula (1) wherein R1, R2, R3, X, Y, Z, A, B, G1, m, and n are defined in the description. The present invention relates also to compositions containing said compounds which are useful for inhibiting kinases such as ALK and methods of treating diseases such as cancer.

Synthesis and structure-activity relationships of nitrobenzyl phosphoramide mustards as nitroreductase-activated prodrugs

A series of nitrobenzyl phosphoramide mustards and their analogs was designed and synthesized to explore their structure-activity relationships as substrates of nitroreductases from Escherichia coli and trypanosomes and as potential antiproliferative and antiparasitic agents. The position of the nitro group on the phenyl ring was important with the 4-nitrobenzyl phosphoramide mustard (1) offering the best combination of enzyme activity and antiproliferative effect against both mammalian and trypanosomatid cells. A preference was observed for halogen substitutions ortho to benzyl phosphoramide mustard but distinct differences were found in their SAR of substituted 4-nitrobenzyl phosphoramide mustards in E. coli nitroreductase-expressing cells and in trypanosomatids expressing endogenous nitroreductases.

Substituent effects on the kinetics of reductively-initiated fragmentation of nitrobenzyl carbamates designed as triggers for bioreductive prodrugs

4-Nitrobenzyl carbamates are of interest as triggers for bioreductive drugs, particularly in conjunction with the E. coli B nitroreductase, which efficiently reduces them to the corresponding hydroxylamines. These then fragment to release highly toxic amine-based toxins. While many 4-nitrobenzyl carbamate derivatives have been evaluated as bioreductive drugs, there has been no systematic study of substituent effects on the rate of this fragmentation (which should be as fast as possible following reduction). We therefore prepared a series of 2-, 3- and α-substituted 4-[N-methyl-N-(4-nitrobenzyloxycarbonyl)amino]phenylacetamides as model compounds to study these effects. The majority of the carbamates were prepared by in situ formation of the chloroformate of the appropriate 4-nitrobenzyl alcohol and reaction with methyl 4-(methylamino)phenylacetate, followed by ester hydrolysis and 1,1′-carbonyl-diimidazole (CDI) mediated coupling with N,N-dimethylaminoethylamine. The hydroxylamines were generated by 60Co γ-ray irradiation of the nitro compounds in aqueous phosphate-buffered-propan-2-ol. The reactions were analysed by reverse-phase HPLC to determine the maximum half-life (Mt1/2) of the hydroxylamines generated, and the extent of release of amine from these after 10 half-lives (t∞). The parent (unsubstituted) hydroxylaminobenzyl carbamate had a Mt1/2 of 16 min under these conditions, while that of the corresponding α-methyl analogue was 9.5 min. Electron-donating substituents on the benzyl ring also accelerated fragmentation, with the data being fitted to the equation log(Mt1/2) = 0.57σ + 1.30, where σ represents σp for 2-substituents and σm for 3-substituents. The acceleration of fragmentation of the hydroxylamines with increasing substituent electron-donation is consistent with the proposed mechanism, and is presumably due to stabilisation of the developing positive charge on the benzylic carbon. The extent of release of amine (t∞) also increased with increasing substituent electron-donation. These data suggest that the standard 4-nitrobenzyl carbamate trigger for nitroreductase enzyme (NTR) prodrugs can likely be improved on, by increasing the rate of fragmentation by the use of α-methyl and/or electron-donating benzyl substituents. The Royal Society of Chemistry 1999.