7508-99-8

Usage

Uses

Used in Pharmaceutical Industry:
1-(3-Fluorophenyl)-1H-pyrrole-2,5-dione is used as a pharmaceutical intermediate for the synthesis of various drug candidates. Its unique structure and properties may contribute to the development of new therapeutic agents with improved efficacy and selectivity.
Used in Agrochemical Industry:
In the agrochemical industry, 1-(3-Fluorophenyl)-1H-pyrrole-2,5-dione may be utilized as a key intermediate in the synthesis of agrochemicals, such as pesticides and herbicides. Its specific properties could enhance the performance and selectivity of these products, leading to more effective and environmentally friendly solutions for crop protection.
Used in Medicinal Chemistry:
1-(3-Fluorophenyl)-1H-pyrrole-2,5-dione serves as a valuable building block in medicinal chemistry, enabling the design and synthesis of novel bioactive compounds. Its heterocyclic nature and the presence of a fluorine atom on the phenyl ring may impart specific biological activities, making it a promising candidate for the development of new drugs and therapeutic agents.
Used in Drug Development:
In the field of drug development, 1-(3-Fluorophenyl)-1H-pyrrole-2,5-dione may be employed as a lead compound for the discovery of new pharmaceuticals. Its unique structural features and potential biological activities can be further optimized and modified to enhance its therapeutic potential, leading to the development of innovative treatments for various diseases and conditions.

InChI:InChI=1/C10H6FNO2/c11-7-2-1-3-8(6-7)12-9(13)4-5-10(12)14/h1-6H

Upstream product

• 372-19-0 meta-fluoroaniline 
• 198879-81-1 C₁₀H₈FNO₃ 
• 6633-31-4 N-(3-Fluorphenyl)-maleamsaeure 
• 108-31-6 maleic anhydride 

Downstream Products

• 1258548-41-2 2-(1-(3-fluorophenyl)-2,5-dioxopyrrolidin-3-yl)-2-methylpropanal 
• 327099-22-9 C₂₆H₁₅ClFNO₅ 
• 1229020-28-3 C₁₄H₁₂FN₃O₄ 
• 1041480-18-5 C₂₄H₁₆FNO₃ 

Relevant academic research and scientific papers

The discovery, design and synthesis of potent agonists of adenylyl cyclase type 2 by virtual screening combining biological evaluation

Adenylate cyclases (ACs), play a critical role in the conversion of adenosine triphosphate (ATP) into the second messenger cyclic adenosine monophosphate (cAMP). Studies have indicated that adenylyl cyclase type 2 (AC2) is potential drug target for many diseases, however, up to now, there is no AC2-selective agonist reported. In this research, docking-based virtual screening with the combination of cell-based biological assays have been performed for discovering novel potent and selective AC2 agonists. Virtual screening disclosed a novel hit compound 8 as an AC2 agonist with EC50 value of 8.10 μM on recombinant human hAC2 + HEK293 cells. The SAR (structure activity relationship) based on the derivatives of compound 8 was further explored on recombinant AC2 cells and compound 73 was found to be the most active agonist with the EC50 of 90 nM, which is 160-fold more potent than the reported agonist Forskolin and could selectively activate AC2 to inhibit the expression of Interleukin-6. The discovery of a new class of AC2-selective agonists would provide a novel chemical probe to study the physiological function of AC2.

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.

Discovery and structural optimization of pyrazole derivatives as novel inhibitors of Cdc25B

Structural optimization and preliminary structure-activity relationship studies of a series of N-substituted maleimide fused-pyrazole analogues with Cdc25B inhibitory activity, starting from a high-throughput screening hit, are illustrated. A simplified 3,5-diacyl pyrazole analogue was obtained as the most potent compound (118, IC50 = 0.12 μM) with a 270-fold increase in potency.

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.

Design and synthesis of a novel DNA-encoded chemical library using Diels-Alder cycloadditions

DNA-encoded chemical libraries are increasingly being employed for the identification of binding molecules to protein targets of pharmaceutical relevance. Here, we describe the synthesis and characterization of a DNA-encoded chemical library, consisting of 4000 compounds generated by Diels-Alder cycloaddition reactions. The compounds were encoded with unique DNA fragments which were generated through a stepwise assembly process and serve as amplifiable bar codes for the identification and relative quantification of library members.