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    Biological Activities of the Natural Coumarins from Apiaceae Plants
    (Acg Publications, 2023) Tosun, Fatma; Biltekin, Sevde Nur; Karadag, Ayse Esra; Mihoglugil, Feyyaz; Akalgan, Demet; Miski, Mahmut
    Nineteen natural coumarins; badrakemin (1), colladonin (2), 14'-acetoxybadrakemin (3), anatolicin (4), 14'-hydroxycolladonin (5), badrakemone (6), karatavicinol (7), 14'-acetoxybadrakemone (8), 14'-acetoxycolladonin (9), colladonin acetate (10), deltoin (11), smyrnioridin (12), isoimperatorin (13), oxypeucedanin (14), bergapten (15), osthol (16), 4'-senecioyloxyostol (17), neopapillarine (18), and scoparone (19) were tested against U87MG, A549, and PC3 cancer cell lines as well as against healthy human embryonic kidney cell line, HEK293. Colladonin (2) was found to have IC50 values of 12.6 and 11.58 & mu;M in A549 and PC3 cell lines, respectively. Deltoin (11) and 14'-acetoxybadrakemin (3) were found to have an IC50 value of 9.92 & mu;M and 11.85 & mu;M against the U87MG cell line, respectively. Remarkably, these compounds show very low cytotoxicity against the healthy human embryonic kidney cell line, HEK293. In addition to the cytotoxic activity, nineteen natural coumarins were tested for their inhibitory activity against 5-LOX, collagenase, and elastase enzymes.& COPY; 2023 ACG Publications. All rights reserved
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    Butyrylcholinesterase-inhibiting natural coumarin molecules as potential leads
    (Elsevier Ltd, 2021) Orhan, İlkay Erdoğan; Tosun, Fatma; Şenol Deniz, Fatma Sezer; Eren, Gökçen; Mıhoğlugil, Feyyaz; Akalgan, Demet; Miski, Mahmut
    Seventeen 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.