Premium
Novel NHC Precursors: Synthesis, Characterization, and Carbonic Anhydrase and Acetylcholinesterase Inhibitory Properties
Author(s) -
Aktaş Aydın,
Taslimi Parham,
Gülçin İlhami,
Gök Yetkin
Publication year - 2017
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.201700045
Subject(s) - carbonic anhydrase , chemistry , carbonic anhydrase i , acetylcholinesterase , acetazolamide , enzyme , stereochemistry , tacrine , proton nmr , isozyme , enzyme inhibitor , active site , cholinesterase , medicinal chemistry , biochemistry , anesthesia , medicine
Three series of imidazolidinium ligands (NHC precursors) substituted with 4‐vinylbenzyl, 2‐methyl‐1,4‐benzodioxane, and N ‐propylphthalimide were synthesized. N ‐Heterocyclic carbene (NHC) precursors were prepared from N ‐alkylimidazoline and alkyl halides. The novel NHC precursors were characterized by 1 H NMR, 13 C NMR, FTIR spectroscopy, and elemental analysis techniques. The enzymes inhibition activities of the NHC precursors were investigated against the cytosolic human carbonic anhydrase I and II isoenzymes (hCA I and II) and the acetylcholinesterase (AChE) enzyme. The inhibition parameters (IC 50 and K i values) were calculated by spectrophotometric method. The inhibition constants ( K i ) were found to be in the range of 166.65–635.38 nM for hCA I, 78.79–246.17 nM for hCA II, and 23.42–62.04 nM for AChE. Also, the inhibitory effects of the novel synthesized NHCs were compared to acetazolamide as a clinical CA isoenzymes inhibitor and tacrine as a clinical cholinergic enzymes inhibitor.