Novel N-propylphthalimide- and 4-vinylbenzyl-substituted benzimidazole salts: Synthesis, characterization, and determination of their metal chelating effects and inhibition profiles against acetylcholinesterase and carbonic anhydrase enzymes


SARı Y., AKTAŞ A., Taslimi P., GÖK Y., GÜLÇİN İ.

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, vol.32, no.1, 2018 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 32 Issue: 1
  • Publication Date: 2018
  • Doi Number: 10.1002/jbt.22009
  • Journal Name: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Keywords: acetylcholinesterase, benzimidazole, carbonic anhydrase, metal chelating, N-heterocyclic carbene precursors, ERYTHROCYTES IN-VITRO, SILVER COMPLEXES SYNTHESIS, ANTIOXIDANT ACTIVITY, ISOENZYMES I, HETEROCYCLIC CARBENES, ISOZYMES I, HCA I, DERIVATIVES, BUTYRYLCHOLINESTERASE, BROMOPHENOLS
  • Inonu University Affiliated: Yes

Abstract

The novel N-propylphthalimide-substituted and 4-vinylbenzyl-substituted N-heterocyclic carbene (NHC) precursors were synthesized by N-substituted benzimidazolium with aryl halides. The novel N-propylphthalimide-substituted and 4-vinylbenzyl-substituted NHC precursors have been characterized by using H-1 NMR, C-13 NMR, FTIR spectroscopy, and elemental analysis techniques. They were tested for the inhibition of AChE and hCA enzymes and demonstrated efficient inhibition profiles with K-i values in the range of 351.0-1269.9 nM against hCA I, 346.6-1193.1 nM against hCA II, and 19.0-76.3 nM against AChE. On the other hand, acetazolamide, a clinically used molecule, utilized as CA inhibitor, obtained a K-i value of 1246.7 nM against hCA I and 1407.6 nM against hCA II. Additionally, tacrine inhibited AChE and obtained a K-i value of 174.6 nM.