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dc.contributor.authorOzgun, Dilan Ozmen
dc.contributor.authorYamali, Cem
dc.contributor.authorGul, Halise Inci
dc.contributor.authorTaslimi, Parham
dc.contributor.authorGulcin, Ilhami
dc.contributor.authorYanik, Telat
dc.contributor.authorSupuran, Claudiu T.
dc.date.accessioned2019-06-13T07:01:30Z
dc.date.available2019-06-13T07:01:30Z
dc.date.issued2016
dc.identifier.urihttp://hdl.handle.net/11772/1391
dc.description.abstractThe effects of isatin Mannich bases incorporating (1-[piperidin-1-yl (P1)/morpholin-4-yl (P2)/N-methylpiperazin-1-yl (P3)]methyl)-1H-indole-2,3-dione) moieties against human (h) carbonic anhydrase (CA, EC 4.2.1.1) isoenzymes hCA I and hCA II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes were evaluated. P1-P3 demonstrated impressive inhibition profiles against AChE and BChE and also inhibited both CAs at nanomolar level. These inhibitory effects were more powerful in all cases than the reference compounds used for all these enzymes. This study suggests that isatin Mannich bases P1-P3 are good candidate compounds especially for the development of new cholinesterase inhibitors since they were 2.2-5.9 times better inhibitors than clinically used drug Tacrine.en_US
dc.language.isoengen_US
dc.publisherInformaen_US
dc.relation.isversionof10.3109/14756366.2016.1149479en_US
dc.rightsinfo:eu-repo/semantics/restrictedAccessen_US
dc.subjectAcetylcholinesteraseen_US
dc.subjectMannich basesen_US
dc.subjectButyrylcholinesteraseen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectIsatinen_US
dc.titleInhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesteraseen_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.volume31en_US
dc.identifier.issue6en_US
dc.identifier.startpage1498en_US
dc.identifier.endpage1501en_US


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