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dc.contributor.authorKocyigit, Umit M.
dc.contributor.authorBudak, Yakup
dc.contributor.authorEliguzel, Fikret
dc.contributor.authorTaslimi, Parham
dc.contributor.authorKilic, Deryanur
dc.contributor.authorGulcin, Ilhami
dc.contributor.authorCeylan, Mustafa
dc.date.accessioned2019-07-27T12:10:23Z
dc.date.accessioned2019-07-28T09:39:51Z
dc.date.available2019-07-27T12:10:23Z
dc.date.available2019-07-28T09:39:51Z
dc.date.issued2017
dc.identifier.issn0365-6233
dc.identifier.issn1521-4184
dc.identifier.urihttps://dx.doi.org/10.1002/ardp.201700198
dc.identifier.urihttps://hdl.handle.net/20.500.12418/6592
dc.descriptionWOS: 000416834000003en_US
dc.descriptionPubMed ID: 29134667en_US
dc.description.abstractIn the present study, human carbonic anhydrase (hCA) enzyme was purified and characterized from fresh blood human red cells by Sepharose-4B-l-tyrosine-sulfanilamide affinity gel chromatography. Secondly, a series of new tetrabromo chalcone derivatives containing 4,7-methanoisoindol-1,3-dione (2a-i) were synthesized from the addition of Br-2 to related chalcone derivatives (1a-i). The structures of the new molecules (2a-i) were confirmed by means of H-1 NMR, C-13 NMR and elemental analysis. Finally, the inhibitory effects of 2a-i on CA activities were investigated using the esterase method under in vitro conditions. The compounds 2a-i exhibited excellent inhibitory effects, in the low nanomolar range, with K-i values in the range of 11.30-21.22nM against hCA I and in the range of 8.21-12.86nM against hCA II. Our findings suggest that the new compounds 2a-i have superior inhibitory effect over acetazolamide (AZA), which is used as clinical CA inhibitor, with obtained K-i values of 34.50 and 28.93nM against the hCA I and II isozymes, respectively. In addition to the inhibition assays, molecular modeling approaches were implemented for prediction of the binding affinities of compounds 2a and 2c, which had the highest inhibition effects, against the hCA I and II isozymes.en_US
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TUBITAK) [111T990]; Gaziosmanpasa University Scientific Research Projects Commission [BAP2011/62]en_US
dc.description.sponsorshipThe authors are indebted to the Scientific and Technological Research Council of Turkey (TUBITAK Project No: 111T990) and Gaziosmanpasa University Scientific Research Projects Commission (Project No: BAP2011/62) for their financial support.en_US
dc.language.isoengen_US
dc.publisherWILEY-V C H VERLAG GMBHen_US
dc.relation.isversionof10.1002/ardp.201700198en_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectChalconeen_US
dc.subjectEnzyme inhibitionen_US
dc.subjectMolecular docking simulationsen_US
dc.subjectMolecular modelingen_US
dc.titleSynthesis and Carbonic Anhydrase Inhibition of Tetrabromo Chalcone Derivativesen_US
dc.typearticleen_US
dc.relation.journalARCHIV DER PHARMAZIEen_US
dc.contributor.department[Kocyigit, Umit M. -- Eliguzel, Fikret] Cumhuriyet Univ, Vocat Sch Hlth Serv, Sivas, Turkey -- [Budak, Yakup -- Ceylan, Mustafa] Gaziosmanpasa Univ, Dept Chem, Fac Arts & Sci, TR-60250 Tokat, Turkey -- [Taslimi, Parham -- Gulcin, Ilhami] Ataturk Univ, Dept Chem, Fac Sci, Erzurum, Turkey -- [Kilic, Deryanur] Aksaray Univ, Dept Chem, Art & Sci Fac, Aksaray, Turkeyen_US
dc.contributor.authorID, deryanur -- 0000-0002-9115-136X; GULCIN, Ilhami -- 0000-0001-5993-1668en_US
dc.identifier.volume350en_US
dc.identifier.issue12en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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