An Efficient Ionic Liquid Mediated Synthesis, Cholinesterase Inhibitory Activity and Molecular Modeling Study of Novel Piperidone Embedded α ,β-Unsaturated Ketones

Abstract

A series of hitherto unreported piperidone embedded α,β-unsaturated ketones were synthesized efficiently in ionic solvent and evaluated for cholinesterase inhibitory activities against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes. Most of the synthesized compounds displayed good enzyme inhibition; therein compounds 7i and 7f displayed significant activity against AChE with IC50 values of 1.47 and 1.74 µM, respectively. Compound 6g showed the highest BChE inhibitory potency with IC50 value of 3.41 µM, being 5 times more potent than galanthamine. Molecular modeling simulation was performed using AChE and BChE receptors extracted from crystal structure of human AChE and human BChE to determine the amino acid residues involved in the binding interaction of synthesized compounds and their relevant receptors.

One‐pot Synthesis of Novel Spirooxindoles as Antibacterial and Antioxidant Agents

“…It has reported that the equimolar amounts of isatins 1 , sarcosine and 4‐aryl‐4‐oxo‐2‐butenoic acids 2 or chalcones 3 in boiling aqueous methanol (1:3) afforded exclusively the spirooxindoles via The multicomponent 1,3‐dipolar cycloaddition (MCDC). The authors wanted to prepare the new spirooxindoline derivatives having a high HOMO energy value to increase the efficiency as antioxidant reagents.…”

A Facile Ionic Liquid Promoted Synthesis, Cholinesterase Inhibitory Activity and Molecular Modeling Study of Novel Highly Functionalized Spiropyrrolidines

“…As a part of our ongoing research project aimed at identifying potential cholinesterase inhibitors for AD therapy [ 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 ], we report here our efforts in search of novel potent cholinesterase inhibitors using dipolar cycloaddition strategy. In addition, molecular modeling studies were also performed to disclose the binding modes of the most active inhibitors to the amino acid residues that compose the active site of the AChE enzyme.…”