AI Article Synopsis
- The study examined the inhibitory effects of harmane, naucledine, and dihydrodeglycocadambine on butyrylcholinesterase (BChE), showing over 80% inhibition at 100 µg/mL for isolated fractions from plants.
- Among the compounds, harmane was found to be the most potent inhibitor with an IC value of 22.08 µM, while naucledine and dihydrodeglycocadambine had slightly higher IC values.
- Docking studies indicated effective binding of the compounds to BChE, while paralysis assays demonstrated that harmane and naucledine reduced paralysis in a transgenic model, although the effects were modest.
Article Abstract
This study investigated the butyrylcholinesterase (BChE) inhibitory activity of harmane (), naucledine (), and dihydrodeglycocadambine () isolated from fractions F7 and F9 of . Both fractions demonstrated significant inhibition, exceeding 80%, against BChE at 100 µg/mL. Compound , is the most potent inhibitor, exhibiting an IC value of 22.08 µM, followed by and (IC 23.96 and 30.32 µM, respectively). Docking studies revealed that and effectively bind to BChE, with binding energies of -51.24 and -57.17 kcal/mol, respectively. Kinetic analysis of indicated mixed-mode inhibition of BChE, with a of 6.08 μM. In the paralysis assay, showed a weak delay in paralysis and reduced the paralysis ratio from 72.59 ± 4.7% to 60.00 ± 7.0% (12.59% reduction) followed by with 70.00 ± 1.7% (2.59% reduction) compared with negative standard (DMSO 0.1%) on human amyloid -protein in a transgenic (CL4176) model.
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| http://dx.doi.org/10.1080/14786419.2024.2394096 | DOI Listing |
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