Butyrylcholinesterase-inhibiting natural coumarin molecules as potential leads

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dc.authorid0000-0003-2533-5141
dc.contributor.authorErdoğan Orhan, İlkay
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.accessioned2021-06-04T06:02:09Z
dc.date.available2021-06-04T06:02:09Z
dc.date.issued2021
dc.departmentİstanbul Medipol Üniversitesi, Eczacılık Fakültesi, Eczacılık Meslek Bilimleri Bölümü, Farmakognozi Ana Bilim Dalı
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.
dc.identifier.citationErdoğan Orhan, İ., Tosun, F., Şenol Deniz, F. S., Eren, G., Mıhoğlugil, F., Akalgan, D. ... Miski, M. (2021). Butyrylcholinesterase-inhibiting natural coumarin molecules as potential leads. Phytochemistry Letters, 44, 48-54. https://dx.doi.org/10.1016/j.phytol.2021.05.001
dc.identifier.doi10.1016/j.phytol.2021.05.001
dc.identifier.endpage54
dc.identifier.issn1874-3900
dc.identifier.issn1876-7486
dc.identifier.scopusqualityQ2
dc.identifier.startpage48
dc.identifier.urihttps://dx.doi.org/10.1016/j.phytol.2021.05.001
dc.identifier.urihttps://hdl.handle.net/20.500.12511/7029
dc.identifier.volume44
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Ltd
dc.relation.ispartofPhytochemistry Lettersen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/embargoedAccess
dc.subjectAlzheimer's Disease
dc.subjectCholinesterase
dc.subjectCoumarin
dc.subjectMolecular Docking
dc.subjectTyrosinase
dc.titleButyrylcholinesterase-inhibiting natural coumarin molecules as potential leads
dc.typeArticle

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