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dc.contributor.authorTurker, Ferhat
dc.contributor.authorCelepci, Duygu Barut
dc.contributor.authorCelepci, Duygu Barut
dc.contributor.authorAktaş, Aydın
dc.contributor.authorTaslimi, Parham
dc.contributor.authorGök, Yetkin
dc.contributor.authorAygün, Muhittin
dc.contributor.authorGülçin, İlhami
dc.date.accessioned2019-04-29T08:03:30Z
dc.date.available2019-04-29T08:03:30Z
dc.date.issued2018-07
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1002/ardp.201800029
dc.identifier.urihttp://hdl.handle.net/11772/1124
dc.description.abstractmeta-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.isoengen_US
dc.publisherWileyen_US
dc.relation.isversionof10.1002/ardp.201800029en_US
dc.rightsinfo:eu-repo/semantics/restrictedAccessen_US
dc.subjectN-heterocyclic carbene precursorsen_US
dc.subjectGlycosidaseen_US
dc.subjectAcetylcholinesteraseen_US
dc.subjectButyrylcholinesteraseen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectEnzyme inhibitionen_US
dc.titleMeta-Cyanobenzyl substituted benzimidazolium salts: Synthesis, characterization, crystal structure and carbonic anhydrase, -glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory propertiesen_US
dc.typearticleen_US
dc.relation.journalArchiv der Pharmazieen_US
dc.contributor.departmentBartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümüen_US
dc.identifier.volume351en_US
dc.identifier.issue7en_US
dc.identifier.startpagee1800029en_US


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