dc.contributor.author | Turker, Ferhat | |
dc.contributor.author | Celepci, Duygu Barut | |
dc.contributor.author | Celepci, Duygu Barut | |
dc.contributor.author | Aktaş, Aydın | |
dc.contributor.author | Taslimi, Parham | |
dc.contributor.author | Gök, Yetkin | |
dc.contributor.author | Aygün, Muhittin | |
dc.contributor.author | Gülçin, İlhami | |
dc.date.accessioned | 2019-04-29T08:03:30Z | |
dc.date.available | 2019-04-29T08:03:30Z | |
dc.date.issued | 2018-07 | |
dc.identifier.uri | https://onlinelibrary.wiley.com/doi/full/10.1002/ardp.201800029 | |
dc.identifier.uri | http://hdl.handle.net/11772/1124 | |
dc.description.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. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Wiley | en_US |
dc.relation.isversionof | 10.1002/ardp.201800029 | en_US |
dc.rights | info:eu-repo/semantics/restrictedAccess | en_US |
dc.subject | N-heterocyclic carbene precursors | en_US |
dc.subject | Glycosidase | en_US |
dc.subject | Acetylcholinesterase | en_US |
dc.subject | Butyrylcholinesterase | en_US |
dc.subject | Carbonic anhydrase | en_US |
dc.subject | Enzyme inhibition | en_US |
dc.title | Meta-Cyanobenzyl substituted benzimidazolium salts: Synthesis, characterization, crystal structure and carbonic anhydrase, -glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory properties | en_US |
dc.type | article | en_US |
dc.relation.journal | Archiv der Pharmazie | en_US |
dc.contributor.department | Bartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümü | en_US |
dc.identifier.volume | 351 | en_US |
dc.identifier.issue | 7 | en_US |
dc.identifier.startpage | e1800029 | en_US |