Alkaloids of Zephyranthes citrina (Amaryllidaceae) and their implication to Alzheimer's disease: Isolation, structural elucidation and biological activity

Varování

Publikace nespadá pod Lékařskou fakultu, ale pod Farmaceutickou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	KOHELOVA E. MARIKOVA J. KORABECNY J. HULCOVA D. KUCERA T. JUN D. CHLEBEK J. JENCO J. SAFRATOVA M. HRABINOVA M. RITOMSKA A. MALANÍK Milan PERINOVA R. BREITEROVA K. KUNES J. NOVAKOVA L. OPLETAL L. CAHLIKOVA L.
Rok publikování	2021
Druh	Článek v odborném periodiku
Časopis / Zdroj	Bioorganic Chemistry
Fakulta / Pracoviště MU	Farmaceutická fakulta
Citace
www	https://reader.elsevier.com/reader/sd/pii/S0045206820318654?token=5E47B1A8AADF6BF05D1AAF363BAF7C93AC087C9BDDAE841A51EAC2BBE4E3BF467F787C1AC7BE0F078B20D8FC896C9179&originRegion=eu-west-1&originCreation=20210930052405
Doi	http://dx.doi.org/10.1016/j.bioorg.2020.104567
Klíčová slova	Zephyranthes citrina; Amaryllidaceae; Alkaloids; Narcieliine; Alzheimer's disease; Docking studies
Popis	Twenty known Amaryllidaceae alkaloids of various structural types, and one undescribed alkaloid of narcikachnine-type, named narcieliine (3), have been isolated from fresh bulbs of Zephyranthes citrina. The chemical structures of the isolated alkaloids were elucidated by a combination of MS, HRMS, 1D and 2D NMR, and CD spectroscopic techniques, and by comparison with literature data. The absolute configuration of narcieliine (3) has also been determined. Compounds isolated in a sufficient quantity were evaluated for their in vitro acetylcholinesterase (AChE; E.C. 3.1.1.7), butyrylcholinesterase (BuChE; E.C. 3.1.1.8), and prolyl oligopeptidase (POP; E.C. 3.4.21.26) inhibition activities. Significant human AChE/BuChE (hAChE/hBuChE) inhibitory activity was demonstrated by the newly described alkaloid narcieliine (3), with IC50 values of 18.7 +/- 2.3 mu M and 1.34 +/- 0.31 mu M, respectively. This compound is also predicted to cross the blood-brain barrier (BBB) through passive diffusion. The in vitro data were further supported by in silico studies of 3 in the active site of hAChE/hBuChE.