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dc.contributor.authorIlhami, Gulcin
dc.contributor.authorMalahat, Abbasova
dc.contributor.authorTaslimi, Parham
dc.contributor.authorZubeyir, Huyut
dc.contributor.authorLeyla, Safarova
dc.contributor.authorAfsun, Sujayev
dc.contributor.authorVagif, Farzaliyev
dc.contributor.authorSukru, Beydemir
dc.contributor.authorSaleh H., Alwasel
dc.contributor.authorClaudiu T., Supuran
dc.date.accessioned2019-05-17T07:41:09Z
dc.date.available2019-05-17T07:41:09Z
dc.date.issued2017
dc.identifier.urihttp://hdl.handle.net/11772/1191
dc.description.abstractCompounds containing nitrogen and sulfur atoms can be widely used in various fields such as industry, medicine, biotechnology and chemical technology. Therefore, the reactions of aminomethylation and alkoxymethylation of mercaptobenzothiazole, mercaptobenzoxazole and 2-aminothiazole were developed. Additionally, the alkoxymethyl derivatives of mercaptobenzoxazole and 2-aminothiazole were synthesized by a reaction with hemiformals, which are prepared by the reaction of alcohols and formaldehyde. In this study, the inhibitory effects of these molecules were investigated against acetylcholinesterase (AChE), butyrylcholinesterase (BChE) enzymes and carbonic anhydrase I, and II isoenzymes (hCA I and II). Both hCA isoenzymes were significantly inhibited by the recently synthesized molecules, with Ki values in the range of 58-157 nM for hCA I, and 81-215 nM for hCA II. Additionally, the Ki parameters of these molecules for BChE and AChE were calculated in the ranges 23-88 and 18-78 nM, respectively.en_US
dc.language.isoengen_US
dc.publisherInformaen_US
dc.relation.isversionof10.1080/14756366.2017.1368019en_US
dc.rightsinfo:eu-repo/semantics/restrictedAccessen_US
dc.subjectAcetylcholinesteraseen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectMercaptobenzothiazoleen_US
dc.subjectMercaptobenzoxazoleen_US
dc.subjectButyrylcholinesteraseen_US
dc.titleSynthesis and biological evaluation of aminomethyl and alkoxymethyl derivatives as carbonic anhydrase, acetylcholinesterase and butyrylcholinesterase inhibitorsen_US
dc.typearticleen_US
dc.relation.journalJournal of Enzyme Inhibition and Medicinal Chemistryen_US
dc.contributor.departmentBartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümüen_US
dc.identifier.volume32en_US
dc.identifier.issue1en_US
dc.identifier.startpage1174en_US
dc.identifier.endpage1182en_US


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