6633-31-4

Usage

Uses

Used in Pharmaceutical Industry:
(Z)-4-((3-fluorophenyl)amino)-4-oxobut-2-enoic acid is used as a chemical compound for the development of new drugs. Its unique structure, which includes a fluorophenyl group and an amino group, may contribute to its potential as a building block for more complex molecules in the pharmaceutical industry.
Used in Drug Development:
(Z)-4-((3-fluorophenyl)amino)-4-oxobut-2-enoic acid is used as a building block for constructing more complex molecules. Its potential applications in the pharmaceutical industry may be further explored through research and development, as it could be a valuable component in the creation of new drugs or therapeutic agents.
Used in Research and Development:
(Z)-4-((3-fluorophenyl)amino)-4-oxobut-2-enoic acid is used as a subject of study for understanding its potential applications and effects. Further research may be needed to fully comprehend the compound's properties and how it can be effectively utilized in various pharmaceutical applications.

InChI:InChI=1/C10H8FNO3/c11-7-2-1-3-8(6-7)12-9(13)4-5-10(14)15/h1-6H,(H,12,13)(H,14,15)

Upstream product

• 108-31-6 maleic anhydride 
• 372-19-0 meta-fluoroaniline 

Downstream Products

• 7508-99-8 1-(3-fluorophenyl)-1H-pyrrole-2,5-dione 

Relevant academic research and scientific papers

Synthesis and biological evaluation of novel benzylidene-succinimide derivatives as noncytotoxic antiangiogenic inhibitors with anticolorectal cancer activity in vivo

A novel series of benzylidene-succinimide derivatives were synthesized, characterized and evaluated for their cytotoxicities against HCT116, and SW480 cancer cells and NCM460 normal human cells. Their antiangiogenic capabilities were evaluated using a chick chorioallantoic membrane (CAM) assay. The compound, XCF-37b, was selected as the most potent antiangiogenic inhibitor with noncytotoxicity to evaluate the pharmacological effects on human umbilical vein endothelial cells (HUVECs) and cancer cells in vivo and in vitro. The results showed that XCF-37b inhibited HT29-cell colon tumor growth in vivo, without showing cytotoxicity against the five other cancer cell lines in vitro. Experiments confirmed that XCF-37b had obvious antiangiogenic activity by HUVEC migration and invasion and rat aortic ring angiogenesis ex vivo. Mechanism studies showed that XCF-37b inhibited the AKT/mTOR and VEGFR2 signaling pathways, as evidenced by decreased expressions of phosphor-AKT (p-AKT), p-mTOR, p-VEGFR2 (Tyr175), p-Src (Tyr416), p-FAK (Tyr925), and p-Erk1/2 (Thr202/Tyr204). Moreover, XCF-37b significantly decreased the protein expressions of matrix metalloproteinase-2 (MMP-2), MMP-9 and hypoxia-inducible factor-1α (HIF-1α). XCF-37b generally regulated angiogenic inhibition through several regulatory pathways, without significantly interfering with colorectal cancer cell growth.

DABCO-catalyzed [3+2] cycloaddition reactions of azomethine imines with N-aryl maleimides: Facile access to dinitrogen-fused heterocycles

DABCO-catalyzed [3+2] cycloaddition of azomethine imines with maleimides has been developed. This method could efficiently furnish dinitrogen-fused tetracyclic heterocycles in high levels of regioselectivity and with good yields.

Synthesis and in vitro evaluation of N-substituted maleimide derivatives as selective monoglyceride lipase inhibitors

The endocannabinoid 2-arachidonoylglycerol (2-AG) plays a major role in many physiological processes, and its action is quickly terminated via enzymatic hydrolysis catalyzed by monoglyceride lipase (MGL). Regulating its endogenous level could offer therapeutic opportunities; however, few selective MGL inhibitors have been described so far. Here, we describe the synthesis of N-substituted maleimides and their pharmacological evaluation on the recombinant human fatty acid amide hydrolase (FAAH) and on the purified human MGL. A few N-arylmaleimides were previously described (Saario, S. M.; Salo, O. M.; Nevalainen, T.; Poso, A.; Laitinen, J. T.; Jarvinen, T.; Niemi, R. Characterization of the Sulfhydryl-Sensitive Site in the Enzyme Responsible for Hydrolysis of 2-Arachidonoylglycerol in Rat Cerebellar Membranes. Chem. Biol. 2005, 12, 649-656) as MGL inhibitors, and along these lines, we present a new set of maleimide derivatives that showed low micromolar IC50 and high selectivity toward MGL vs FAAH. Then, structure-activity relationships have been investigated and, for instance, 1-biphenyl-4-ylmethylmaleimide inhibits MGL with an IC50 value of 790 nM. Furthermore, rapid dilution experiments reveal that these compounds act as irreversible inhibitors. In conclusion, N-substituted maleimides constitute a promising class of potent and selective MGL inhibitors.

Substituent chemical shifts of N-arylsuccinanilic acids, N-arylsuccinimides, N-arylmaleanilic acids, and N-arylmaleimides

NMR spectra of a series of N-arylsuccinanilic acids, N-arylsuccinimides, N-arylmaleanilic acids, and N-arylmaleimides were examined to estimate the electronic effect of the amide and imide groups on the chemical shifts of the hydrogen and carbon nuclei of the benzene ring.

INFLUENCE OF MEDIUM AND SUBSTITUENTS ON ACYLATION OF AROMATIC AMINES AND THEIR POLYMERIC ANALOGS WITH MALEIC ANHYDRIDE

Correlation relationships describing the influence of substituents and solvents on the rate of acylation of aromatic amines and their polymeric analogs with maleic anhydride have been derived.