Butyrylcholinesterase-inhibiting natural coumarin molecules as potential leads

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dc.authoridDemet Akalgan / 0000-0001-6956-163Xen_US
dc.authorscopusidDemet Akalgan / 56529576000
dc.authorwosidDemet Akalgan / EKB-6148-2022
dc.contributor.authorOrhan, İlkay Erdoğan
dc.contributor.authorTosun, Fatma
dc.contributor.authorŞenol Deniz, Fatma Sezer
dc.contributor.authorEren, Gökçen
dc.contributor.authorMıhoğlugil, Feyyaz
dc.contributor.authorAkalgan, Demet
dc.contributor.authorMiski, Mahmut
dc.date.accessioned2021-06-07T06:02:06Z
dc.date.available2021-06-07T06:02:06Z
dc.date.issued2021en_US
dc.departmentİstinye Üniversitesi, Eczacılık Fakültesi, Eczacılık Meslek Bilimleri Bölümüen_US
dc.description.abstractSeventeen natural coumarin derivatives; badrakemin (1), 14?-acetoxybadrakemin (2), badrakemone (3), 14?-acetoxybadrakemone (4), colladonin (5), colladonin acetate (6), 14?-acetoxycolladonin (7), karatavicinol (8), deltoin (9), smyrnioridin (10), marmesin (11), osthol (12), oxypeucedanin (13), oxypeucedanin hydrate (14), isoimperatorin (15), scopoletin (16), and umbelliprenin (17), were tested against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), the sister enzymes that play a critical role in the pathology of Alzheimer's disease as well as tyrosinase (TYR) as the target for Parkinson's disease. The tested coumarins were more selective against BChE, where the coumarins 2, 5, 8, and 15 (IC50 = 30.3 ?M, 29.2 ?M, 37.2 ?M, and 50.1 ?M, respectively) displayed higher BChE inhibition than the reference (galanthamine, IC50 = 60.2 ?M) at 100 ?g/mL. Only four coumarins (2, 5, 9, and 15) showed inhibition against AChE. Binding conformations of the coumarins (2, 5, 8, 9, and 15) within the active sites of AChE and BChE were explored via molecular docking experiments. The docked compounds were oriented by the interactions with the oxyanion hole and the peripheral anionic site residues of AChE/BChE. The coumarin derivatives 1–17 was found to have no or low inhibition (2.03 ± 0.92 %–12.91 ± 0.40 %) against TYR at 100 ?g/mL. Our findings revealed that coumarins could be promising lead compounds for designing novel anti-Alzheimer drug candidates.en_US
dc.identifier.citationOrhan, I. E., Tosun, F., Deniz, F. S. S., Eren, G., Mıhoğlugil, F., Akalgan, D., & Miski, M. (2021). Butyrylcholinesterase-inhibiting natural coumarin molecules as potential leads. Phytochemistry Letters, 44, 48-54.en_US
dc.identifier.doi10.1016/j.phytol.2021.05.001en_US
dc.identifier.endpage54en_US
dc.identifier.issn1874-3900en_US
dc.identifier.scopus2-s2.0-85106394205en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage48en_US
dc.identifier.urihttps://doi.org/10.1016/j.phytol.2021.05.001
dc.identifier.urihttps://hdl.handle.net/20.500.12713/1780
dc.identifier.volume44en_US
dc.identifier.wosWOS:000693417900008en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorAkalgan, Demet
dc.language.isoenen_US
dc.publisherElsevier Ltden_US
dc.relation.ispartofPhytochemistry Lettersen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAlzheimer's Diseaseen_US
dc.subjectCholinesteraseen_US
dc.subjectCoumarinen_US
dc.subjectMolecular Dockingen_US
dc.subjectTyrosinaseen_US
dc.titleButyrylcholinesterase-inhibiting natural coumarin molecules as potential leadsen_US
dc.typeArticleen_US

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