31385-19-0

Basic information

• Product Name: 1,2,6-trimethyl-1,2-dihydroquinoline
• CAS NO: 31385-19-0
• Molecular Formula: C₁₂H₁₄N*I
• Molecular Weight: 173.2542
• Mol File: 31385-19-0.mol
• Article Data: 2

Chemical Properties

• Boiling Point: 282°C at 760 mmHg
• Flash Point: 113.6°C
• Density: 0.979g/cm³
• Vapor Pressure: 0.00345mmHg at 25°C
• Refractive Index: 1.544
• CAS DataBase Reference: 1,2,6-trimethyl-1,2-dihydroquinoline(CAS DataBase Reference)
• NIST Chemistry Reference: 1,2,6-trimethyl-1,2-dihydroquinoline(31385-19-0)
• EPA Substance Registry System: 1,2,6-trimethyl-1,2-dihydroquinoline(31385-19-0)

Safety Data

• Hazardous Substances Data: 31385-19-0(Hazardous Substances Data)

Usage

Type of compound

Synthetic derivative of quinoline

Usage

Antioxidant and stabilizer in the rubber industry

Function

Prevents degradation and extends the lifespan of rubber products

Mechanism

Reacts with and neutralizes free radicals causing oxidation and degradation of rubber materials

Result

Improved heat and oxygen resistance

Additional applications

Production of adhesives, sealants, and other polymer-based materials

Purpose in other industries

Improves stability and performance of these materials

Status

Effective and widely-used additive in the rubber industry

Benefit

Protects and enhances the durability of rubber products

Upstream product

• 877-43-0 2,6-dimethylquinoline 
• 74-88-4 methyl iodide 

Downstream Products

• 67943-66-2 C₁₃H₁₃NS₂ 
• 74020-12-5 1,6-dimethyl-2-<2-methylthio-2-(1-morpholino)vinyl>quinolinium iodide 

Relevant articles and documents

Structure-Activity Relationship for Small Molecule Inhibitors of Nicotinamide N-Methyltransferase

Nicotinamide N-methyltransferase (NNMT) is a fundamental cytosolic biotransforming enzyme that catalyzes the N-methylation of endogenous and exogenous xenobiotics. We have identified small molecule inhibitors of NNMT with >1000-fold range of activity and developed comprehensive structure-Activity relationships (SARs) for NNMT inhibitors. Screening of N-methylated quinolinium, isoquinolinium, pyrididium, and benzimidazolium/benzothiazolium analogues resulted in the identification of quinoliniums as a promising scaffold with very low micromolar (IC50 à 1 μM) NNMT inhibition. Computer-based docking of inhibitors to the NNMT substrate (nicotinamide)-binding site produced a robust correlation between ligand-enzyme interaction docking scores and experimentally calculated IC50 values. Predicted binding orientation of the quinolinium analogues revealed selective binding to the NNMT substrate-binding site residues and essential chemical features driving protein-ligand intermolecular interactions and NNMT inhibition. The development of this new series of small molecule NNMT inhibitors direct the future design of lead drug-like inhibitors to treat several metabolic and chronic disease conditions characterized by abnormal NNMT activity.