55618-86-5

Upstream product

• 74-88-4 methyl iodide 
• 186581-53-3 diazomethane 
• 38186-54-8 1,2,3,4-tetrahydro-9-acridinecarboxylic acid 
• 91-56-5 indole-2,3-dione 
• 108-94-1 cyclohexanone 

Downstream Products

• 6854-08-6 1,2,3,4-tetrahydro-9-acridinecarboxaldehyde 

Relevant academic research and scientific papers

Quinoline-4-methyl esters as human nonpancreatic secretory phospholipase A2 inhibitors

A series of novel fused heterocycle methyl esters were designed and synthesized as human nonpancreatic secretory phospholipase A2 (hnps-PLA2) competitive inhibitors. Among the 22 synthesized compounds, 17 quinoline-4-methyl esters displayed hnps-PLA2 inhibition activity in the in vitro bioassay. The IC50 value for the best compound 3o was 1.5 μM. The structure-inhibition-activity relationships of the compounds were studied using molecular docking.

Development of molecular probes for the identification of extra interaction sites in the mid-gorge and peripheral sites of butyrylcholinesterase (BuChE). Rational design of novel, selective, and highly potent BuChE inhibitors

Tacrine heterobivalent ligands were designed as novel and reversible inhibitors of cholinesterases. On the basis of the investigation of the active site gorge topology of butyrylcholinesterase (BuChE) and acetylcholinesterase (AChE) and by using flexible docking procedures, molecular modeling studies formulated the hypothesis of extra interaction sites in the active gorge of hBuChE, namely, a mid-gorge interaction site and a peripheral interaction site. The design strategy led to novel BuChE inhibitors, balancing potency and selectivity. Among the compounds identified, the heterobivalent ligand 4m, containing an amide nitrogen and a sulfur atom at the 8-membered tether level, is one of the most potent and selective BuChE inhibitors described to date. The novel inhibitors, bearing postulated key features, validated the hypothesis of the presence of extra interaction sites within the hBuChE active site gorge.