20994-09-6

Basic information

• Product Name: Carbamothioic acid, dimethyl-, O-(4-cyanophenyl) ester
• CAS NO: 20994-09-6
• Molecular Formula: C10H10N2OS
• Molecular Weight: 206.268
• Mol File: 20994-09-6.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: Carbamothioic acid, dimethyl-, O-(4-cyanophenyl) ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamothioic acid, dimethyl-, O-(4-cyanophenyl) ester(20994-09-6)
• EPA Substance Registry System: Carbamothioic acid, dimethyl-, O-(4-cyanophenyl) ester(20994-09-6)

Safety Data

• Hazardous Substances Data: 20994-09-6(Hazardous Substances Data)

Upstream product

• 767-00-0 4-cyanophenol 
• 16420-13-6 N,N-Dimethylthiocarbamoyl chloride 
• 66300-17-2 4-cyanophenyl chlorothionoformate 
• 124-40-3 dimethyl amine 

Downstream Products

• 36801-01-1 4-cyanobenzenethiol 
• 19290-43-8 4-cyanophenyl-S,N,N-dimethyl thiocarbamate 

Relevant articles and documents

Microwave-mediated Newman-Kwart rearrangement in water

For the first time the unimolecular Newman-Kwart rearrangement is performed in pure water. The elevated temperatures required for the 1,3-aryl shift are easily accomplished by microwave irradiation. Differently functionalized substrates underline the expe

6-ARYLALKYLAMINO- 2,3,4,5-TETRAHYDRO-1H-BENZO[D]AZEPINES AS 5-HT2C RECEPTOR AGONISTS

The present invention provides 6-substituted 2,3,4,5-tetrahydro-lH- benzo[d]azepines of Formula (I) as selective 5-HT2c receptor agonists for the treatment of 5-HT2c associated disorders including obesity, obsessive/compulsive disorder, depression, and anxiety, where, R6 is -NR10R11, where R10 is substituted phenylalkyl or substituted pyridylalkyl and other substituents are as defined in the specification.

Effects of aromatic thiols on thiol-disulfide interchange reactions that occur during protein folding

The folding of disulfide containing proteins from denatured protein to native protein involves numerous thiol-disulfide interchange reactions. Many of these reactions include a redox buffer, which is a mixture of a thiol (RSH) and the corresponding disulfide (RSSR). The relationship between the structure of RSH and its efficacy in folding proteins in vitro has been investigated only to a limited extent. Reported herein are the effects of aliphatic and especially aromatic thiols on reactions that occur during protein folding. Aromatic thiols may be particularly efficacious as their thiol pKa values and reactivities match those of the in vivo catalyst, protein disulfide isomerase (PDI). This investigation correlates the thiol pKa values of aromatic thiols with their reactivities toward small molecule disulfides and the protein insulin. The thiol pKa values of nine para-substituted aromatic thiols were measured; a Hammett plot constructed using σp- values yielded ρ = -1.6 ± 0.1. The reactivities of aromatic and aliphatic thiols with 2-pyridyldithioethanol (2-PDE), a small molecule disulfide, were determined. A plot of reactivity versus pKa of the aromatic thiols had a slope (β) of 0.9. The ability of these thiols to reduce (unfold) the protein insulin correlates strongly with their ability to reduce 2-PDE. Since the reduction of protein disulfides occurs during protein folding to remove mismatched disulfides, aromatic thiols with high pKa values are expected to increase the rate not only of protein unfolding but protein folding as well.