1268444-83-2

Usage

Uses

Used in Pharmaceutical Industry:
1-(4-chloro-3-fluorophenyl)cyclopropanecarboxylic acid is utilized as an intermediate in the synthesis of various drugs and active pharmaceutical ingredients. Its cyclopropane ring structure and the presence of chloro and fluoro substitutions contribute to its value in creating novel and effective medications.
Used in Research and Development:
1-(4-chloro-3-fluorophenyl)cyclopropanecarboxylic acid also serves as a research tool for studying cyclopropane-containing compounds and their potential pharmacological applications. The unique properties of 1-(4-chloro-3-fluorophenyl)cyclopropanecarboxylic acid make it a valuable asset in the exploration of new drug candidates and the enhancement of existing ones.

Upstream product

• 251570-03-3 2-(4-chloro-3-fluorophenyl)acetonitrile 
• 1265476-80-9 1-(4-chloro-3-fluorophenyl)cyclopropanecarbonitrile 

Downstream Products

• 1252641-41-0 (4R)-1-{[1-(4-chloro-3-fluorophenyl)cyclopropyl]carbonyl}-4-[(2-chlorophenyl)sulfonyl]-N-(1-cyanocyclopropyl)-L-prolinamide 
• 1268445-06-2 (4R)-1-{[1-(4-chloro-3-fluorophenyl)cyclopropyl]carbonyl}-4-{[2-chloro-4-(2,2,2-trifluoroethoxy)phenyl]sulfonyl}-N-(1-cyanocyclopropyl)-L-prolinamide 

Relevant academic research and scientific papers

Chiral Bidentate Boryl Ligand Enabled Iridium-Catalyzed Enantioselective C(sp3)-H Borylation of Cyclopropanes

We herein report an Ir-catalyzed enantioselective C(sp3)-H borylation of cyclopropanecarboxamides using a chiral bidentate boryl ligand for the first time. A variety of substrates with α-quaternary carbon centers could be compatible in this reaction to provide β-borylated products with good to excellent enantioselectivities. We have also demonstrated that the borylated products can be used as versatile precursors engaging in stereospecific transformations of C-B bonds, including the synthesis of a bioactive compound Levomilnacipran.

Systematic investigation of halogen bonding in protein-ligand interactions

Halogen bonding triggers activity: Increasing binding affinity was observed for a series of covalent human Cathepsin L inhibitors by exchanging an aryl ring H atom with Cl, Br, and I, which undergo halogen bonding with the C=O group of Gly61 in the S3 pocket of the enzyme. Fluorine, in contrast, strongly avoids halogen bonding (see scheme). The strong distance and angle dependence of halogen bonding was confirmed for biological systems. Copyright