Investigation of in vitro and in silico effects of some novel carbazole Schiff bases on human carbonic anhydrase isoforms I and II

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dc.authoridAdem, Sevki/0000-0003-2146-5870
dc.authoridCALISIR, Umit/0000-0001-7699-2008
dc.authoridCICEK, Baki/0000-0003-1257-1188
dc.contributor.authorCamadan, Yasemin
dc.contributor.authorCicek, Baki
dc.contributor.authorAdem, Sevki
dc.contributor.authorCalisir, Umit
dc.contributor.authorAkkemik, Ebru
dc.date.accessioned2024-12-24T19:28:11Z
dc.date.available2024-12-24T19:28:11Z
dc.date.issued2022
dc.departmentSiirt Üniversitesi
dc.description.abstractCarbonic anhydrases (CAs, EC4.2.1.1) are metalloenzymes that catalyse reversible hydration reaction of carbon dioxide to bicarbonate and protons. In recent years, there has been a great interest in inhibitors/activators of carbonic anhydrase isoenzymes. Therefore, we investigated the effects of four different carbazole Schiff base derivatives, which are believed to have a potential to be used as a drug, on human carbonic anhydrase (hCA) isoenzymes I and II under in vitro conditions. The IC50 values of carbazole Schiff base derivatives were found to be in the range of 32.09-151.2 mu M for hCA isoenzyme I and 21.82-40.54 mu M for hCA isoenzyme II. Among all compounds, (E)-3-(((9-Octyl-9H-carbazole-3-yl)imino)methyl)benzene-1,2-diol (C3) had the strongest inhibitory effect on hCA isoenzyme II. It was determined that 2,3,4-trimethoxy and 4-hydroxy phenyl containing carbazole compounds have selective inhibition against hCA II isoenzyme. Docking studies were performed against hCA I and II receptors using induced-fit docking method. The compounds had affinity scores varying from -7.74 +/- 0.27 to -6.27 +/- 0.07 kcal/mol for hCA I and from -8.04 +/- 0.17 to -7.27 +/- 0.18 kcal/mol for hCA II. Communicated by Ramaswamy H. Sarma
dc.description.sponsorshipScientific Research Project of Bali kesir University of Turkey [BAP.2015.0001, BAP.2017/181]
dc.description.sponsorshipThis work was supported by a grant from the Scientific Research Project of Bali kesir University of Turkey [Grant Number: BAP.2015.0001 and Grant Number: BAP.2017/181].
dc.identifier.doi10.1080/07391102.2021.1892527
dc.identifier.endpage6973
dc.identifier.issn0739-1102
dc.identifier.issn1538-0254
dc.identifier.issue15
dc.identifier.pmid33645441
dc.identifier.scopus2-s2.0-85101883574
dc.identifier.scopusqualityQ1
dc.identifier.startpage6965
dc.identifier.urihttps://doi.org/10.1080/07391102.2021.1892527
dc.identifier.urihttps://hdl.handle.net/20.500.12604/6941
dc.identifier.volume40
dc.identifier.wosWOS:000623962400001
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTaylor & Francis Inc
dc.relation.ispartofJournal of Biomolecular Structure & Dynamics
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_20241222
dc.subjectCarbazole
dc.subjectcarbonic anhydrase
dc.subjectdocking
dc.subjectesterase activity
dc.subjectinhibition
dc.subjectSchiff bases
dc.titleInvestigation of in vitro and in silico effects of some novel carbazole Schiff bases on human carbonic anhydrase isoforms I and II
dc.typeArticle

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