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oai:ebyu-rdlopen.rawdatalibrary.net:ebyu/138052026-10-18T21:13:31Zopenairedrivercom_ebyu_10000col_ebyu_10001

Synthesis and biological evaluation of novel tris-chalcones as potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and α-glycosidase inhibitorsBurmaoglu, SerdarYilmaz, Ali OsmanPolat, M. FatihKaya, RüyaGulcin, İlhamiAlgul, OztekinAcetylcholinesteraseButyrylcholinesteraseCarbonic anhydraseTris-chalconeα-glycosidaseCarbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase InhibitorsChalconesCholinesterase InhibitorsGlycoside Hydrolase InhibitorsHumansMolecular Structure1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (2 fluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (2,3 difluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (2,4 difluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (2,4,5 trifluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (2,5 difluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (3 fluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (3,4 difluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (3,5 difluorophenyl)prop 2 en 1 one]1,1',1'' (2,4,6 trimethoxybenzene 1,3,5 triyl)tris[3 (4 fluorophenyl)prop 2 en 1 one]acarboseacetazolamidecarbonate dehydratase Icarbonate dehydratase IIcarbonate dehydratase inhibitorchalcone derivativecholinesterasecholinesterase inhibitorA novel class of fluoro-substituted tris-chalcones derivatives (5a-5i) was synthesized from phloroglucinol and corresponding benzaldehydes. A three step synthesis method was followed for the production of these tris-chalcone compounds. The structures of the newly synthesized compounds (5a-5i) were confirmed on the basis of IR, 1 H NMR, 13 C NMR, and elemental analysis. The compounds’ inhibitory activities were tested against human carbonic anhydrase I and II isoenzymes (hCA I and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase (α-Gly). These chalcone derivatives had K i values in the range of 19.58–78.73 nM for hCA I, 12.23–41.70 nM for hCA II, 1.09–6.84 nM for AChE, 8.30–32.30 nM for BChE and 0.93 ± 0.20–18.53 ± 5.06 nM against α-glycosidase. These results strongly support the promising nature of the tris-chalcone scaffold as selective carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α-glycosidase inhibitor. Overall, due to these derivatives’ inhibitory potential on the tested enzymes, they are promising drug candidates for the treatment of diseases like glaucoma, leukemia, epilepsy; Alzheimer's disease; type-2 diabetes mellitus that are associated with high enzymatic activity of carbonic anhydrase, acetylcholine esterase, butyrylcholinesterase, and α-glycosidase. © 2018Academic Press Inc.2019Articlehttps://rdlopen.rawdatalibrary.net/r/ebyu/13805https://doi.org/10.1016/j.bioorg.2018.12.0350045-2068enBioorganic Chemistryinfo:eu-repo/semantics/openAccessinfo:eu-repo/semantics/articlehttps://ebyu-rdlopen.rawdatalibrary.net/tr/items/ebyu/13805