Highly potent cholinesterase inhibition of geranylated xanthones from Garcinia fusca and molecular docking studies

Fitoterapia. 2020 Oct:146:104637. doi: 10.1016/j.fitote.2020.104637. Epub 2020 May 27.

Abstract

Three new oxygenated xanthones, fuscaxanthones L-N (1-3), and 14 known xanthones 4-17, together with the other known metabolites 18-20 were isolated from the stem barks of Garcinia fusca Pierre. Their chemical structures were determined based on NMR and MS spectroscopic data analysis, as well as single X-ray crystallography. The geranylated compounds, cowanin (13), cowagarcinone E (15), norcowanin (16) and cowanol (17) exhibited potent inhibitions against acetylcholinesterase (AChE) (IC50 0.33-1.09 μM) and butyrylcholinesterase (BChE) (IC50 0.048-1.84 μM), which were more active than the reference drug, galanthamine. Compound 15 was highly potent BChE inhibitor (IC50 0.048 μM) and was 76-fold more potent than the drug. Structure-activity relationship studies indicated that the C-2 prenyl and C-8 geranyl substituents in the tetraoxygenated scaffold are important for high activity. Molecular docking studies revealed that the leads 13 and 15-17 showed similar binding orientations on both enzymes and very well-fitted at the double binding active sites of PAS and CAS with strong hydrophobic interactions from both isoprenyl side chains.

Keywords: Acetylcholinesterase inhibitor; Butyrylcholinesterase inhibitor; Garcinia fusca; Molecular docking; Oxygenated xanthones.

MeSH terms

  • Acetylcholinesterase
  • Butyrylcholinesterase
  • Cholinesterase Inhibitors / isolation & purification
  • Cholinesterase Inhibitors / pharmacology*
  • Garcinia / chemistry*
  • Molecular Docking Simulation
  • Molecular Structure
  • Phytochemicals / isolation & purification
  • Phytochemicals / pharmacology
  • Plant Bark / chemistry*
  • Structure-Activity Relationship
  • Thailand
  • Xanthones / isolation & purification
  • Xanthones / pharmacology*

Substances

  • Cholinesterase Inhibitors
  • Phytochemicals
  • Xanthones
  • Acetylcholinesterase
  • Butyrylcholinesterase