784182-12-3

Basic information

• Product Name: Methyl 1-benzylcyclopentanecarboxylate
• Synonyms: Methyl 1-benzylcyclopentanecarboxylate
• CAS NO: 784182-12-3
• Molecular Formula: C₁₄H₁₈O₂
• Molecular Weight: 218.29152
• Mol File: 784182-12-3.mol

Chemical Properties

• Boiling Point: 295.6±9.0 °C(Predicted)
• Appearance: /
• Density: 1.074±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• CAS DataBase Reference: Methyl 1-benzylcyclopentanecarboxylate(CAS DataBase Reference)
• NIST Chemistry Reference: Methyl 1-benzylcyclopentanecarboxylate(784182-12-3)
• EPA Substance Registry System: Methyl 1-benzylcyclopentanecarboxylate(784182-12-3)

Safety Data

• Hazardous Substances Data: 784182-12-3(Hazardous Substances Data)

Usage

Uses

Used in Flavoring and Fragrance Industry:
Methyl 1-benzylcyclopentanecarboxylate is used as a flavoring agent and fragrance ingredient for its distinctive aromatic properties. It enhances the sensory experience of various consumer products, contributing to their overall appeal and marketability.
Used in Pharmaceutical Synthesis:
In the pharmaceutical industry, Methyl 1-benzylcyclopentanecarboxylate serves as a key intermediate in the synthesis of various organic compounds and pharmaceuticals. Its unique chemical structure allows for the development of new drugs with potential therapeutic benefits.
Used in Chemical Research:
Methyl 1-benzylcyclopentanecarboxylate is also utilized in chemical research for studying the properties and reactions of esters and cyclopentane derivatives. Its versatile structure makes it an ideal candidate for exploring new chemical pathways and developing innovative applications.

Upstream product

• 4630-80-2 methyl cyclopentane carboxylate 
• 100-39-0 benzyl bromide 
• 620-05-3 iodomethylbenzene 

Downstream Products

• 1613145-80-4 1-benzyl-N-(8-quinolinyl)cyclopentanecarboxamide 
• 1613146-08-9 3-phenyl-2-(8-quinolinyl)-2-azaspiro[3.4]-1-octanone 
• 568591-12-8 {(S)-1-[Hydroxy-((R)-1-phenyl-ethylcarbamoyl)-methyl]-pentyl}-carbamic acid 1-benzyl-cyclopentylmethyl ester 
• 568591-11-7 (1-benzyl-cyclopentyl)-methanol 
• 220875-85-4 1-benzylcyclopentane carboxylic acid 

Relevant articles and documents

Copper-catalyzed intramolecular C(sp3)-H and C(sp2)-H amidation by oxidative cyclization

The first copper-catalyzed intramolecular C(sp3)-H and C(sp 2)-H oxidative amidation has been developed. Using a Cu(OAc) 2 catalyst and an Ag2CO3 oxidant in dichloroethane solvent, C(sp3)-H

Nickel-catalyzed site-selective amidation of unactivated C(sp 3)-H bonds

Intramolecular dehydrogenative cyclization of aliphatic amides was achieved on unactivated sp3 carbon atoms by a nickel-catalyzed C-H bond functionalization process with the assistance of a bidentate directing group. The reaction favors the C-H bonds of β-methyl groups over the γ-methyl or β-methylene groups. Additionally, a predominant preference for the β-methyl C-H bonds over the aromatic sp2 C-H bonds was observed. Moreover, this process also allows for the effective functionalization of benzylic secondary sp3 C-H bonds. β-Lactams from nickel catalysis: Intramolecular dehydrogenative cyclization of aliphatic amides was achieved on unactivated sp3 carbon atoms by a nickel-catalyzed C-H bond functionalization process with the assistance of a bidentate directing group (see scheme).

Potent and selective P2-P3 ketoamide inhibitors of cathepsin K with good pharmacokinetic properties via favorable P 1′, P1, and/or P3 substitutions

A series of ketoamides were synthesized and evaluated for inhibitory activity against cathepsin K. Exploration of the interactions between achiral P2 substituents and the cysteine protease based on molecular modeling suggestions resulted in potent cathepsin K inhibitors that demonstrated high selectivity versus cathepsins B, H, and L. Subsequent modifications of the P3, P1, and P1′ moieties afforded orally bioavailable inhibitors. A series of ketoamides were synthesized and evaluated for inhibitory activity against cathepsin K. Exploration of the interactions between achiral P2 substituents and the cysteine protease based on molecular modelling suggestions resulted in potent cathepsin K inhibitors that demonstrated high selectivity versus cathepsins B, H, and L. Subsequent modifications of the P3, P1, and P1′ moieties afforded orally bioavailable inhibitors.

N-Cycloalkanoyl-L-phenylalanine derivatives as VCAM/VLA-4 antagonists.

A systematic structure-activity relationship investigation of the lead compound 1 resulted the identification of several N-[(substituted alkyl)cycloalkanoyl]-4-[((2,6-dichlorophenyl)carbonyl)amino]-L-phenylalanine derivatives as potent VCAM/VLA-4 antagonists. The data are consistent with a model of these compounds in which these alkanoylphenylalanines reside in a compact gauche (-) bioactive conformation.