Clinanthus microstephium, an Amaryllidaceae Species with Cholinesterase Inhibitor Alkaloids: Structure-Activity Analysis of Haemanthamine Skeleton Derivatives.
Acetylcholinesterase
/ chemistry
Alkaloids
/ chemistry
Amaryllidaceae
/ chemistry
Amaryllidaceae Alkaloids
/ chemistry
Binding Sites
Butyrylcholinesterase
/ chemistry
Catalytic Domain
Cholinesterase Inhibitors
/ chemistry
Gas Chromatography-Mass Spectrometry
Inhibitory Concentration 50
Molecular Docking Simulation
Phenanthridines
/ chemistry
Plant Extracts
/ chemistry
Structure-Activity Relationship
Amaryllidaceae
Clinanthus microstephium
alkaloids
biological activity
cholinesterase inhibitors
structure−activity relationship
Journal
Chemistry & biodiversity
ISSN: 1612-1880
Titre abrégé: Chem Biodivers
Pays: Switzerland
ID NLM: 101197449
Informations de publication
Date de publication:
May 2019
May 2019
Historique:
received:
12
12
2018
accepted:
22
02
2019
pubmed:
26
2
2019
medline:
1
6
2019
entrez:
26
2
2019
Statut:
ppublish
Résumé
Plants of the Amaryllidaceae family are well-known (not only) for their ornamental value but also for the alkaloids that they produce. In this report, the first phytochemical study of Clinanthus genus was carried out. The chemical composition of alkaloid fractions from Clinanthus microstephium was analyzed by GC/MS and NMR. Seven known compounds belonging to three structural types of Amaryllidaceae alkaloids were identified. An epimeric mixture of a haemanthamine-type compound (6-hydroxymaritidine) was tested as an inhibitor against acetyl- and butyrylcholinesterase enzymes (AChE and BChE, respectively), two enzymes relevant in the treatment of Alzheimer's disease, with good results. Structure-activity relationships through molecular docking studies with this alkaloid and other structurally related compounds were discussed.
Identifiants
pubmed: 30801949
doi: 10.1002/cbdv.201800662
doi:
Substances chimiques
Alkaloids
0
Amaryllidaceae Alkaloids
0
Cholinesterase Inhibitors
0
Phenanthridines
0
Plant Extracts
0
hemanthamine
466-75-1
Acetylcholinesterase
EC 3.1.1.7
Butyrylcholinesterase
EC 3.1.1.8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1800662Subventions
Organisme : CONICET (Argentina)
Organisme : ANPCYT (Argentina)
Organisme : Ministerio de Ciencia y Tecnología de Córdoba (Argentina)
Organisme : SeCyT-UNC
Informations de copyright
© 2019 Wiley-VHCA AG, Zurich, Switzerland.