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Inhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesterase

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dc.contributor.author Ozgun, Dilan Ozmen
dc.contributor.author Yamali, Cem
dc.contributor.author Gul, Halise Inci
dc.contributor.author Taslimi, Parham
dc.contributor.author Gulcin, Ilhami
dc.contributor.author Yanik, Telat
dc.contributor.author Supuran, Claudiu T.
dc.date.accessioned 2019-06-13T07:01:30Z
dc.date.available 2019-06-13T07:01:30Z
dc.date.issued 2016
dc.identifier.uri http://hdl.handle.net/11772/1391
dc.description.abstract The 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.iso eng en_US
dc.publisher Informa en_US
dc.relation.isversionof 10.3109/14756366.2016.1149479 en_US
dc.rights info:eu-repo/semantics/restrictedAccess en_US
dc.subject Acetylcholinesterase en_US
dc.subject Mannich bases en_US
dc.subject Butyrylcholinesterase en_US
dc.subject Carbonic anhydrase en_US
dc.subject Isatin en_US
dc.title Inhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesterase en_US
dc.type article en_US
dc.relation.journal Journal of Enzyme Inhibition and Medicinal Chemistry en_US
dc.contributor.department Bartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümü en_US
dc.identifier.volume 31 en_US
dc.identifier.issue 6 en_US
dc.identifier.startpage 1498 en_US
dc.identifier.endpage 1501 en_US


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