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meta ‐Cyanobenzyl substituted benzimidazolium salts: Synthesis, characterization, crystal structure and carbonic anhydrase, α‐glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory properties
Author(s) -
Türker Ferhat,
Barut Celepci Duygu,
Aktaş Aydın,
Taslimi Parham,
Gök Yetkin,
Aygün Muhittin,
Gülçin İlhami
Publication year - 2018
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.201800029
Subject(s) - butyrylcholinesterase , chemistry , acetylcholinesterase , carbonic anhydrase , stereochemistry , glycoside hydrolase , carbonic anhydrase i , enzyme , carbonic anhydrase ii , biochemistry , aché
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 1 H NMR, 13 C 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 α‐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 1.01–2.12 nM for AG, 189.56–402.44 nM for hCA I, 112.50–277.37 nM for hCA II, 95.45–352.58 nM for AChE, and 132.91–571.18 nM 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.