31338-28-0

Basic information

• Product Name: 4-[(E)-2-(3,4-dichlorophenyl)-1-ethenyl]pyridine
• CAS NO: 31338-28-0
• Molecular Weight: 250.127
• Mol File: 31338-28-0.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: 4-[(E)-2-(3,4-dichlorophenyl)-1-ethenyl]pyridine(CAS DataBase Reference)
• NIST Chemistry Reference: 4-[(E)-2-(3,4-dichlorophenyl)-1-ethenyl]pyridine(31338-28-0)
• EPA Substance Registry System: 4-[(E)-2-(3,4-dichlorophenyl)-1-ethenyl]pyridine(31338-28-0)

Safety Data

• Hazardous Substances Data: 31338-28-0(Hazardous Substances Data)

Upstream product

• 108-89-4 picoline 
• 6287-38-3 3,4-dichlorobenzaldehyde 

Downstream Products

• 39603-61-7 4-[(E)-2-(3,4-dichlorophenyl)ethenyl]pyridinium chloride 
• 1383439-25-5 4-[(E)-2-(3,4-dichlorophenyl)-1-ethenyl]pyridinium perchlorate 
• 36995-60-5 4-(3,4-dichloro-phenethyl)-pyridine 

Relevant articles and documents

In Situ Assembly of Choline Acetyltransferase Ligands by a Hydrothiolation Reaction Reveals Key Determinants for Inhibitor Design

The potential drug target choline acetyltransferase (ChAT) catalyses the production of the neurotransmitter acetylcholine in cholinergic neurons, T-cells, and B-cells. Herein, we show that arylvinylpyridiniums (AVPs), the most widely studied class of ChAT inhibitors, act as substrate in an unusual coenzyme A-dependent hydrothiolation reaction. This in situ synthesis yields an adduct that is the actual enzyme inhibitor. The adduct is deeply buried in the active site tunnel of ChAT and interactions with a hydrophobic pocket near the choline binding site have major implications for the molecular recognition of inhibitors. Our findings clarify the inhibition mechanism of AVPs, establish a drug modality that exploits a target-catalysed reaction between exogenous and endogenous precursors, and provide new directions for the development of ChAT inhibitors with improved potency and bioactivity.

Flexible N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogues: Synthesis and monoamine oxidase catalyzed bioactivation

Eighteen analogues of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) were synthesized and evaluated as substrates of monoamine oxidase. In general, the flexible analogues, characterized by the presence of a methylene (or ethylene) bridge between the aryl/heteroaryl and tetrahydropyridyl moieties, were better substrates of the enzyme than the conformationally restricted MPTP. It is suggested that the increased oxidative activity of these flexible analogues reflects enhanced binding due to the ability of the C-4-aryl/heteroaryl substituent to gain access to a hydrophobic pocket within the substrate binding site.