853407-59-7

Basic information

• Product Name: 4-benzoyl-2-chloro-3-methylquinoline
• Synonyms: 4-benzoyl-2-chloro-3-methylquinoline
• CAS NO: 853407-59-7
• Molecular Weight: 281.741
• Mol File: 853407-59-7.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: 4-benzoyl-2-chloro-3-methylquinoline(CAS DataBase Reference)
• NIST Chemistry Reference: 4-benzoyl-2-chloro-3-methylquinoline(853407-59-7)
• EPA Substance Registry System: 4-benzoyl-2-chloro-3-methylquinoline(853407-59-7)

Safety Data

• Hazardous Substances Data: 853407-59-7(Hazardous Substances Data)

Upstream product

• 431078-96-5 2-chloro-3-methyl-4-quinolinecarboxylic acid chloride 
• 71-43-2 benzene 
• 91-56-5 indole-2,3-dione 
• 6625-08-7 2-hydroxy-3-methyl-4-quinolinecarboxylic acid 

Relevant articles and documents

Further studies on the interaction of the 5-hydroxytryptamine3 (5-HT3) receptor with arylpiperazine ligands. Development of a new 5-HT3 receptor ligand showing potent acetylcholinesterase inhibitory properties

Novel arylpiperazine derivatives bearing lipophilic probes were designed, synthesized, and evaluated for their potential ability to interact with the 5-hydroxytryptamine3 (5-HT3) receptor. Most of the new compounds show subnanomolar 5-HT3 receptor affinity. Ester 6bc showing a picomolar Ki value is one of the most potent 5-HT 3 receptor ligands so far synthesized. The structure-affinity relationship study suggests the existence of a certain degree of conformational freedom of the amino acid residues interacting with the substituents in positions 3 and 4 of the quipazine quinoline nucleus. Thus, the tacrine-related heterobivalent ligand 60 was designed in an attempt to capitalize on the evidence of such a steric tolerance. Compound 6o shows a nanomolar potency for both the 5-HT3 receptor and the human AChE and represents the first example of a rationally designed high-affinity 5-HT3 receptor ligand showing nanomolar AChE inhibitory activity. Finally, the computational analysis performed on compound 6o allowed the rationalization of the structure-energy determinants for AChE versus BuChE selectivity and revealed the existence of a subsite at the boundary of the 5-HT3 receptor extracellular domain, which could represent a "peripheral" site similar to that evidenced in the AChE gorge.