41116-23-8

Basic information

• Product Name: Carbamic acid, [4-(dimethylamino)phenyl]-, ethyl ester
• CAS NO: 41116-23-8
• Molecular Formula: C11H16N2O2
• Molecular Weight: 208.26
• Mol File: 41116-23-8.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [4-(dimethylamino)phenyl]-, ethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [4-(dimethylamino)phenyl]-, ethyl ester(41116-23-8)
• EPA Substance Registry System: Carbamic acid, [4-(dimethylamino)phenyl]-, ethyl ester(41116-23-8)

Safety Data

• Hazardous Substances Data: 41116-23-8(Hazardous Substances Data)

Upstream product

• 105-39-5 chloroacetic acid ethyl ester 
• 99-98-9 4-amino-N,N-dimethylaniline 
• 64-17-5 ethanol 
• 525-06-4 diphenyl ketene 
• 138-89-6 p-dimethylaminonitrosobenzene 
• 201230-82-2 carbon monoxide 

Downstream Products

• 26271-84-1 hexa-N-methyl-4,4'-ureylene-di-anilinium; bis-dimethyl sulfate 
• 5260-04-8 N,N'-bis[4-(dimethylamino)phenyl]urea 

Relevant articles and documents

Differential functional theory and molecular docking studies of newly synthesized carbamates

Four new carbamates (RZ1–RZ4) were synthesized from different amine moieties through reported methods. The reaction was monitored using thin layer chromatography and characterization was done using m.p., fourier-transform infrared spectroscopy (FTIR), and X-ray diffraction (XRD) techniques. Density functional theory (DFT) studies were carried out using Gaussian 09 software to compare the theoretical and practical parameters of the synthesized compounds. Highest occupied molecular orbital (HOMO) and lowest unoccupied molecular orbital (LUMO) were also drawn to calculate the energy difference between orbitals. In-vitro enzyme inhibition potential against acetylcholine esterase (AChE), butyrylcholine esterase (BChE), and protease was checked through standard protocols that suggested moderate inhibition against selected enzymes. Docking studies were also carried out, which depicted that these compounds have ability to bind on the active site of AChE and BChE.