ArticleJournal of enzyme inhibition and medicinal chemistry2011
Nantenine as an acetylcholinesterase inhibitor: SAR, enzyme kinetics and molecular modeling investigations.
Article in Journal of enzyme inhibition and medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
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- Identification of quinolinyl-containing dual soluble epoxide hydrolase/fatty acid amide hydrolase inhibitors with moderate potency towards acetylcholinesterase.Results in chemistry · 2026Article
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- Novel piperidine-derived amide sEH inhibitors as mediators of lipid metabolism with improved stability.Prostaglandins & other lipid mediators · 2018Article
- Inhibition of Acetylcholinesterase and Butyrylcholinesterase by a Plant Secondary Metabolite Boldine.BioMed research international · 2018Article
- Differential protection of black-seed oil on econucleotidase, cholinesterases and aminergic catabolizing enzyme in haloperidol-induced neuronal damage of male rats.Therapeutic advances in drug safety · 2016Article
- C4 phenyl aporphines with selective h5-HT(2B) receptor affinity.Bioorganic & medicinal chemistry letters · 2015Article
- Aporphinoid antagonists of 5-HT2A receptors: further evaluation of ring A substituents and the size of ring C.Chemical biology & drug design · 2014Article
- Multi-Target-Directed Ligands and other Therapeutic Strategies in the Search of a Real Solution for Alzheimer's Disease.Current neuropharmacology · 2014Article
- A New Route to Azafluoranthene Natural Products via Direct Arylation.European journal of organic chemistry · 2013Article
- New aporphinoid 5-HT2A and α1A antagonists via structural manipulations of nantenine.Bioorganic & medicinal chemistry · 2011Article
- Cytotoxicity of aporphines in human colon cancer cell lines HCT-116 and Caco-2: an SAR study.Bioorganic & medicinal chemistry letters · 2011Article
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3 authors at 2 institutions in 1 country.
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Abstract
Nantenine, as well as a number of flexible analogs, were evaluated for acetylcholinesterase (AChE) inhibitory activity in microplate spectrophotometric assays based on Ellman's method. It was found that the rigid aporphine core of nantenine is an important structural requirement for its anticholinesterase activity. Nantenine showed mixed inhibition kinetics in enzyme assays. Molecular docking experiments suggest that nantenine binds preferentially to the catalytic site of AChE but is also capable of interacting with the peripheral anionic site (PAS) of the enzyme, thus accounting for its mixed inhibition profile. The aporphine core of nantenine may thus be a useful template for the design of novel PAS or dual-site AChE inhibitors. Inhibiting the PAS is desirable for prevention of aggregation of the amyloid peptide Aβ, a major causative factor in the progression of Alzheimer's disease (AD).
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