Ionic liquid mediated synthesis and molecular docking study of novel aromatic embedded Schiff bases as potent cholinesterase inhibitors

Abd Razik BM 1 , Osman H 2 , Basiri A 3 , Salhin A 4 , Kia Y 4 , Ezzat MO 5 Show all authors , Murugaiyah V 6

Affiliations 

  • 1 School of Chemical Sciences, University Sains Malaysia, Minden, 11800 Penang, Malaysia; College of Pharmacy, Al-Mustansiriyah University, Baghdad, Iraq
  • 2 School of Chemical Sciences, University Sains Malaysia, Minden, 11800 Penang, Malaysia. Electronic address: osman.hasnah2012@yahoo.com
  • 3 School of Pharmaceutical Sciences, Universiti Sains Malaysia, Minden, 11800 Penang, Malaysia. Electronic address: alirezaa.basiri@gmail.com
  • 4 School of Chemical Sciences, University Sains Malaysia, Minden, 11800 Penang, Malaysia
  • 5 Center for Drug Research, University Sains Malaysia, Minden, 11800 Penang, Malaysia
  • 6 School of Pharmaceutical Sciences, Universiti Sains Malaysia, Minden, 11800 Penang, Malaysia
Bioorg Chem, 2014 Dec;57:162-168.
PMID: 25462993 DOI: 10.1016/j.bioorg.2014.10.005

Abstract

Novel aromatic embedded Schiff bases have been synthesized in ionic liquid [bmim]Br and evaluated in vitro for their acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes inhibitory activities. Among the newly synthesized compounds, 5f, 5h and 7j displayed higher AChE enzyme inhibitory activities than standard drug, galanthamine, with IC50 values of 1.88, 2.05 and 2.03μM, respectively. Interestingly, all the compounds except for compound 5c displayed higher BChE inhibitories than standard with IC50 values ranging from 3.49 to 19.86μM. Molecular docking analysis for 5f and 7j possessing the most potent AChE and BChE inhibitory activities, disclosed their binding interaction templates to the active site of AChE and BChE enzymes, respectively.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

MeSH terms
Similar publications