25468-87-5

Usage

Uses

Used in Pharmaceutical Synthesis:
3-(3-Fluorophenyl)propanenitrile is utilized as an intermediate in the synthesis of pharmaceuticals, contributing to the development of new drugs and therapeutic agents. Its unique chemical structure allows for the creation of a wide range of medicinal compounds, enhancing the scope of available treatments.
Used in Agrochemical Production:
In the agrochemical industry, 3-(3-Fluorophenyl)propanenitrile serves as an intermediate, playing a crucial role in the synthesis of various agrochemicals. Its incorporation aids in the development of effective pesticides and other agricultural chemicals, supporting crop protection and yield enhancement.
Used as a Building Block in Specialty Chemicals Production:
3-(3-Fluorophenyl)propanenitrile is employed as a building block in the production of specialty chemicals, enabling the creation of unique and high-value chemical products. Its versatility in chemical reactions facilitates the synthesis of a diverse array of specialty compounds for various applications.
Used as a Reagent in Organic Synthesis:
3-(3-FLUOROPHENYL)PROPANENITRILE also functions as a reagent in organic synthesis, where it is involved in a multitude of chemical reactions to produce desired organic compounds. Its reactivity and stability make it a valuable component in the synthesis of complex organic molecules for research and industrial applications.

Upstream product

• 404-96-6 3-(3-fluorophenyl)propanamide 
• 456-48-4 3-Fluorobenzaldehyde 
• 456-47-3 3-fluoro-benzenemethanol 
• 75-05-8 acetonitrile 
• 773837-37-9 sodium cyanide 
• 25017-13-4 1-(2-bromoethyl)-3-fluorobenzene 
• 768-35-4 3-fluorophenylboronic acid 
• 107-13-1 acrylonitrile 
• 456-41-7 1-(Bromomethyl)-3-fluorobenzene 

Downstream Products

• 46457-51-6 2-(3-fluoro-phenethyl)-5,6-dihydro-4H-[1,3]thiazine 
• 104774-86-9 3-(3-fluorophenyl)-propan-1-amine 
• 1562370-36-8 C₂₁H₂₂FN₃O 
• 146386-09-6 3-(3-Benzoyl-thioureido)-4-(3-fluoro-benzyl)-1H-pyrrole-2-carboxylic acid methyl ester 
• 146386-23-4 3-(3-Benzoyl-2-methyl-isothioureido)-4-(3-fluoro-benzyl)-1H-pyrrole-2-carboxylic acid methyl ester 
• 1026331-61-2 3-Amino-4-(3-fluoro-benzyl)-pyrrole-1,2-dicarboxylic acid 1-ethyl ester 2-methyl ester 
• 146385-95-7 3-Amino-4-(3-fluoro-benzyl)-1H-pyrrole-2-carboxylic acid methyl ester 
• 1025883-96-8 3-(3-Fluoro-phenyl)-2-formyl-propionitrile 

Relevant academic research and scientific papers

8-Hydroxyquinolin-2(1H)-one analogues as potential β2-agonists: Design, synthesis and activity study

β2-Agonists that bind to plasmalemmal β2-adrenoceptors causing cAMP accumulation are widely used as bronchodilators in chronic respiratory diseases. Here, we designed and synthesized a group of 8-hydroxyquinolin-2(1H)-one analogues and studied their β2-agonistic activities with a cellular cAMP assay. Compounds B05 and C08 were identified as potent (EC50 2-agonists among the compounds tested. They behaved as partial β2-agonists in non-overexpressed HEK293 cells, and possessed rapid smooth muscle relaxant actions and long duration of action in isolated guinea pig tracheal strip preparations. In summary, B05 and C08 are β2-agonists with potential applicability in chronic respiratory diseases.

A strategy for generating aryl radicals from arylborates through organic photoredox catalysis: Photo-Meerwein type arylation of electron-deficient alkenes

Photoinduced reactions of arylboronic acids with electron deficient alkenes under mild organic photoredox catalysis conditions lead to the formation of Meerwein arylation type adducts via the generation of aryl radicals.

Ametoctradin is a Potent Qo Site Inhibitor of the Mitochondrial Respiration Complex III

Ametoctradin is a new Oomycete-specific fungicide under development by BASF. It is a potent inhibitor of the bc1 complex in mitochondrial respiration. However, its detailed action mechanism remains unknown. In the present work, the binding mode of ametoctradin was first uncovered by integrating molecular docking, MD simulations, and MM/PBSA calculations, which showed that ametoctradin should be a Qo site inhibitor of bc1 complex. Subsequently, a series of new 1,2,4-triazolo[1,5-a]pyrimidine derivatives were designed and synthesized to further understand the substituent effects on the 5- and 6-position of 1,2,4-triazolo[1,5-a]pyrimidine. The calculated binding free energies (ΔGcal) of newly synthesized analogues as Qo site inhibitors correlated very well (R2 = 0.96) with their experimental binding free energies (ΔGexp). Two compounds (4a and 4c) with higher inhibitory activity against porcine SQR than ametoctradin were successfully identified. The structural and mechanistic insights obtained from the present study will provide a valuable clue for future designing of a new promising bc1 inhibitor.

2-AMINOQUINOLINE-BASED COMPOUNDS FOR POTENT AND SELECTIVE NEURONAL NITRIC OXIDE SYNTHASE INHIBITION

Various 2-aminoquinoline compounds as can be used, in vivo or in vitro, for selective inhibition of neuronal nitric oxide synthase.

2-aminoquinoline-based compounds for potent and selective neuronal nitric oxide synthase inhibition

Various 2-aminoquinoline compounds as can be used, in vivo or in vitro, for selective inhibition of neuronal nitric oxide synthase.

Simplified 2-aminoquinoline-based scaffold for potent and selective neuronal nitric oxide synthase inhibition

Since high levels of nitric oxide (NO) are implicated in neurodegenerative disorders, inhibition of the neuronal isoform of nitric oxide synthase (nNOS) and reduction of NO levels are therapeutically desirable. Nonetheless, many nNOS inhibitors mimic l-arginine and are poorly bioavailable. 2-Aminoquinoline-based scaffolds were designed with the hope that they could (a) mimic aminopyridines as potent, isoform-selective arginine isosteres and (b) possess chemical properties more conducive to oral bioavailability and CNS penetration. A series of these compounds was synthesized and assayed against purified nNOS enzymes, endothelial NOS (eNOS), and inducible NOS (iNOS). Several compounds built on a 7-substituted 2-aminoquinoline core are potent and isoform-selective; X-ray crystallography indicates that aminoquinolines exert inhibitory effects by mimicking substrate interactions with the conserved active site glutamate residue. The most potent and selective compounds, 7 and 15, were tested in a Caco-2 assay and showed good permeability and low efflux, suggesting high potential for oral bioavailability.

Monoalkylation of acetonitrile by primary alcohols catalyzed by iridium complexes

The monoalkylation of acetonitrile by primary alcohols was achieved in a one-pot sequence in the presence of iridium catalysts. A diversity of nitriles has been obtained from aryl- and alkyl-methanols in excellent yield.

Structure-based design of inhibitors of purine nucleoside phosphorylase. 1. 9-(Arylmethyl) derivatives of 9-deazaguanine

Purine nucleoside phosphorylase (PNP, EC 2.4.2.1) is a salvage enzyme important to the T-cell-mediated part of the immune system and as such is an important therapeutic target. This paper describes the design, synthesis, and enzymatic evaluation of potent, competitive inhibitors of PNP. Potential inhibitors were designed using the three-dimensional structure of the enzyme in an iterative process that involved interactive computer graphics to model the native enzyme and complexes of it with the inhibitors, Monte Carlo-based conformational searching, and energy minimization. Studies of the enzyme/inhibitor complexes were used to determine priorities of the synthetic efforts. The resulting compounds were then evaluated by determination of their IC50 values and by X-ray diffraction analysis using difference Fourier maps. In this manner, we have developed a series of 9-(arylmethyl)- 9-deazapurines (2-amino-7-(arylmethyl)-4H-pyrrolo[3,2-d]-pyrimidin-4-ones) that are potent, membrane-permeable inhibitors of the enzyme. The IC50 values of these compounds range from 17 to 270 nM (in 1 mM phosphate), with 9-(3,4-dichlorobenzyl)-9-deazaguanine being the most potent inhibitor. X-ray analysis explained the role of the aryl groups and revealed the rearrangement of hydrogen bonds in the binding of the 9-deazaguanines in the active site of PNP relative to the binding of the 8-aminoguanines that results in more potent inhibition of the enzyme.