meta-Cyanobenzyl substituted benzimidazolium salts: Synthesis, characterization, crystal structure and carbonic anhydrase, -glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory properties


TÜRKER F., Celepci D. B., AKTAŞ A., Taslimi P., GÖK Y., Aygun M., ...More

ARCHIV DER PHARMAZIE, vol.351, no.7, 2018 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 351 Issue: 7
  • Publication Date: 2018
  • Doi Number: 10.1002/ardp.201800029
  • Journal Name: ARCHIV DER PHARMAZIE
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Keywords: -glycosidase, acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase, enzyme inhibition, N-heterocyclic carbene precursors, HETEROCYCLIC CARBENE COMPLEXES, ALPHA-GLUCOSIDASE INHIBITORS, ERYTHROCYTES IN-VITRO, II INHIBITION, ISOENZYMES I, HCA I, BROMOPHENOLS, ANTIOXIDANT, DERIVATIVES, ANTICANCER
  • Inonu University Affiliated: Yes

Abstract

meta-Cyanobenzyl-substituted N-heterocyclic carbene (NHC) precursors were synthesized by the reaction of a series of N-(alkyl)benzimidazolium with 3-bromomethyl-benzonitrile. These benzimidazolium salts were characterized by using H-1 NMR, C-13 NMR, FTIR spectroscopy, and elemental analysis techniques. The molecular and crystal structures of 2f and 2g complexes were obtained by using the single-crystal X-ray diffraction method. The derivatives of these novel NHC precursors were effective inhibitors of -glycosidase (AG), the cytosolic carbonic anhydrase I and II isoforms (hCA I and II), butyrylcholinesterase (BChE), and acetylcholinesterase (AChE) with K-i values in the range of 1.01-2.12nM for AG, 189.56-402.44nM for hCA I, 112.50-277.37nM for hCA II, 95.45-352.58nM for AChE, and 132.91-571.18nM for BChE. In the last years, inhibition of the CA enzyme has been considered as a promising factor for pharmacologic intervention in a diversity of disturbances such as obesity, glaucoma, cancer, and epilepsy.