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Chem Biol Interact ; 274: 150-157, 2017 Aug 25.
Article in English | MEDLINE | ID: mdl-28698023

ABSTRACT

Phytochemical investigation of Lycopodium complanatum whole plants led to the isolation of two new serratene-type triterpenoids (1 and 2) along with eight known triterpenoids (3-10). Their structures were established using 1D and 2D NMR spectroscopic techniques and mass spectrometry. These compounds did not inhibit acetylcholinesterases (AChE) and butyrylcholinesterase (BChE), but did inhibit ß-secretase 1 (BACE1). Compounds 1 and 6 showed potent BACE1 inhibition with IC50 values of 2.79 ± 0.28 and 2.49 ± 0.12 µM, respectively. The kinetic study of BACE1 inhibition revealed that compound 1 showed competitive inhibition, whereas 6 showed mixed-type inhibition. Furthermore, molecular docking results showed that the tested inhibitors 1 and 6 exhibited good binding affinities toward BACE1, with binding energies of -8.8 and -10.3 kcal/mol, respectively.


Subject(s)
Acetylcholinesterase/metabolism , Amyloid Precursor Protein Secretases/antagonists & inhibitors , Butyrylcholinesterase/metabolism , Lycopodium/chemistry , Triterpenes/pharmacology , Acetylcholinesterase/chemistry , Amyloid Precursor Protein Secretases/metabolism , Binding Sites , Butyrylcholinesterase/chemistry , Fluorescence Resonance Energy Transfer , Inhibitory Concentration 50 , Kinetics , Lycopodium/metabolism , Magnetic Resonance Spectroscopy , Molecular Conformation , Molecular Docking Simulation , Plant Extracts/chemistry , Protein Binding , Protein Structure, Tertiary , Thermodynamics , Triterpenes/chemistry , Triterpenes/isolation & purification
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