Isolation of cholinesterase and β-secretase 1 inhibiting compounds from Lycopodiella cernua
Copyright policy )Isolation of cholinesterase and β-secretase 1 inhibiting compounds from Lycopodiella cernua
Three new serratene-type triterpenoids (1-3) and a new hydroxy unsaturated fatty acid (13) together with nine known compounds (4-12) were isolated from Lycopodiella cernua. The chemical structures were established using NMR, MS, and Mosher's method. Compound 13 showed the most potent inhibitory activity against acetylcholinesterase (AChE) with an IC50 value of 0.22μM. For butyrylcholinesterase (BChE) inhibitory activity, 5 showed the most potent activity with an IC50 value of 0.42μM. Compound 2 showed the most potent activity with an IC50 of 0.23μM for BACE-1 inhibitory activity. The kinetic activities were investigated to determine the type of enzyme inhibition involved. The types of AChE inhibition shown by compounds 4, 5, and 13 were mixed; BChE inhibition by 5 was competitive, while 2 and 6 showed mixed-types. In addition, molecular docking studies were performed to investigate the interaction of these compounds with the pocket sites of AChE. The docking results revealed that the tested inhibitors 3, 4, and 13 were stably present in several pocket domains of the AChE residue.
- Pukyong National University Korea (Republic of)
- Catholic University of Daegu Korea (Republic of)
- Kyungpook National University Korea (Republic of)
Molecular Structure, Plant Extracts, Triterpenes, Molecular Docking Simulation, Kinetics, Structure-Activity Relationship, Butyrylcholinesterase, Catalytic Domain, Acetylcholinesterase, Fatty Acids, Unsaturated, Aspartic Acid Endopeptidases, Humans, Lycopodiaceae, Protease Inhibitors, Cholinesterase Inhibitors, Amyloid Precursor Protein Secretases, Protein Binding
Molecular Structure, Plant Extracts, Triterpenes, Molecular Docking Simulation, Kinetics, Structure-Activity Relationship, Butyrylcholinesterase, Catalytic Domain, Acetylcholinesterase, Fatty Acids, Unsaturated, Aspartic Acid Endopeptidases, Humans, Lycopodiaceae, Protease Inhibitors, Cholinesterase Inhibitors, Amyloid Precursor Protein Secretases, Protein Binding
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