2026-10-19T01:03:56Zhttps://ebyu-rdlopen.rawdatalibrary.net/oai/request

oai:ebyu-rdlopen.rawdatalibrary.net:ebyu/131892026-10-18T21:13:30Zopenairedrivercom_ebyu_10000col_ebyu_10001

Synthesis of novel tris-chalcones and determination of their inhibition profiles against some metabolic enzymesBurmaoglu, SerdarYilmaz, Ali OsmanPolat, M. FatihKaya, RüyaGulcin, İlhamiAlgul, Oztekinacetylcholinesterasebutyrylcholinesterasecarbonic anhydraseTris-chalconeα-glycosidaseCarbonic Anhydrase InhibitorsCarbonic AnhydrasesChalconesCholinesterase InhibitorsHumanscarbonate dehydratasecarbonate dehydratase inhibitorchalcone derivativecholinesterasecholinesterase inhibitorchemistryhumansynthesisIn this study, we report the synthesis of novel tris-chalcones and testing of human carbonic anhydrase I, and II isoenzymes (hCA I, and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase (α-Gly) inhibitors for the development of novel chalcone structures towards for treatment of some diseases. The compounds demonstrated K i values between 13.6 ± 1.1 and 50.0 ± 17.1 nM on hCA I, 9.9 ± 0.8 and 39.5 ± 15.1 nM on hCA II, 3.1 ± 0.2 and 20.1 ± 1.9 nM on AChE, 4.9 ± 0.4 and 14.7 ± 5.2 nM on BChE and 3.9 ± 0.2 and 22.4 ± 10.7 nM on α-Gly enzymes. The results revealed that novel tris-chalcones can have promising drug potential for glaucoma, leukaemia, epilepsy; Alzheimer’s disease that was associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes. © 2019 Informa UK Limited, trading as Taylor & Francis Group.Taylor and Francis Ltd.2021Articlehttps://rdlopen.rawdatalibrary.net/r/ebyu/13189https://doi.org/10.1080/13813455.2019.16232651381-3455enArchives of Physiology and Biochemistryinfo:eu-repo/semantics/openAccessinfo:eu-repo/semantics/articlehttps://ebyu-rdlopen.rawdatalibrary.net/tr/items/ebyu/13189