943111-83-9

Basic information

• Product Name: Methyl 1-(4-fluorophenyl)cyclopropanecarboxylate
• Synonyms: Cyclopropanecarboxylic acid, 1-(4-fluorophenyl)-, Methyl ester;Methyl 1-(4-fluorophenyl)cyclopropanecarboxylate
• CAS NO: 943111-83-9
• Molecular Formula: C₁₁H₁₁FO₂
• Molecular Weight: 194.2022432
• Mol File: 943111-83-9.mol

Chemical Properties

• Appearance: /
• Storage Temp.: Room temperature.
• CAS DataBase Reference: Methyl 1-(4-fluorophenyl)cyclopropanecarboxylate(CAS DataBase Reference)
• NIST Chemistry Reference: Methyl 1-(4-fluorophenyl)cyclopropanecarboxylate(943111-83-9)
• EPA Substance Registry System: Methyl 1-(4-fluorophenyl)cyclopropanecarboxylate(943111-83-9)

Safety Data

• Hazardous Substances Data: 943111-83-9(Hazardous Substances Data)

Upstream product

• 133284-48-7 1-(4-fluorophenyl)cyclopropane-1-carboxamide 
• 97009-67-1 1-(4-fluorophenyl)cyclopropane-1-carbonitrile 
• 459-22-3 4-fluorophenylacetonitrile 
• 34837-84-8 4-fluorobenzeneacetic acid methyl ester 
• 67-56-1 methanol 
• 773100-29-1 1-(4-fluorophenyl)cyclopropane-1-carboxylic acid 

Downstream Products

• 633317-83-6 1-(4-fluorophenyl)cyclopropanecarbohydrazide 

Relevant articles and documents

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Distinctive molecular inhibition mechanisms for selective inhibitors of human 11β-hydroxysteroid dehydrogenase type 1

11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1) catalyzes the NADPH dependent interconversion of inactive cortisone to active cortisol. Excess 11β-HSD1 or cortisol leads to insulin resistance and metabolic syndrome in animal models and in humans. Inhibiting 11β-HSD1 activity signifies a promising therapeutic strategy in the treatment of Type 2 diabetes and related diseases. Herein, we report two highly potent and selective small molecule inhibitors of human 11β-HSD1. While compound 1, a sulfonamide, functions as a simple substrate competitive inhibitor, compound 2, a triazole, shows the kinetic profile of a mixed inhibitor. Co-crystal structures reveal that both compounds occupy the 11β-HSD1 catalytic site, but present distinct molecular interactions with the protein. Strikingly, compound 2 interacts much closer to the cofactor NADP+ and likely modifies its binding. Together, the structural and kinetic analyses demonstrate two distinctive molecular inhibition mechanisms, providing valuable information for future inhibitor design.