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Structure Elucidation and Cholinesterase Inhibition Activity of Two New Minor Amaryllidaceae Alkaloids
J. Maříková, AA. Mamun, LA. Shammari, J. Korábečný, T. Kučera, D. Hulcová, J. Kuneš, M. Malaník, M. Vašková, E. Kohelová, L. Nováková, L. Cahlíková, M. Pour
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články
Grantová podpora
SVV UK 260 548, SVV UK 260 547
Grantová Agentura, Univerzita Karlova
VT2019-2021
University Hradec Králové
00179906
University Hospital Hradec Kralove
CZ.02.1.01/0.0/0.0/16_019/0000841
European Regional Development Fund
NLK
Directory of Open Access Journals
od 1997
Free Medical Journals
od 1997
PubMed Central
od 2001
Europe PubMed Central
od 2001
ProQuest Central
od 1997-01-01
Open Access Digital Library
od 1997-01-01
Medline Complete (EBSCOhost)
od 2009-03-01
Health & Medicine (ProQuest)
od 1997-01-01
- MeSH
- alkaloidy amarylkovitých chemie farmakologie MeSH
- alkaloidy chemie farmakologie MeSH
- Alzheimerova nemoc MeSH
- butyrylcholinesterasa chemie ultrastruktura MeSH
- cholinesterasové inhibitory chemie farmakologie MeSH
- cholinesterasy chemie ultrastruktura MeSH
- cirkulární dichroismus MeSH
- katalytická doména účinky léků MeSH
- lidé MeSH
- molekulární struktura MeSH
- simulace molekulového dockingu MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
Two new minor Amaryllidaceae alkaloids were isolated from Hippeastrum × hybridum cv. Ferrari and Narcissus pseudonarcissus cv. Carlton. The chemical structures were identified by various spectroscopic (one- and two-dimensional (1D and 2D) NMR, circular dichroism (CD), high-resolution mass spectrometry (HRMS) and by comparison with literature data of similar compounds. Both isolated alkaloids were screened for their human acetylcholinesterase (hAChE) and butyrylcholinesterase (hBuChE) inhibition activity. One of the new compounds, a heterodimer alkaloid of narcikachnine-type, named narciabduliine (2), showed balanced inhibition potency for both studied enzymes, with IC50 values of 3.29 ± 0.73 µM for hAChE and 3.44 ± 0.02 µM for hBuChE. The accommodation of 2 into the active sites of respective enzymes was predicted using molecular modeling simulation.
Citace poskytuje Crossref.org
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