| Autor: |
Osman N; Department of Chemistry, Faculty of Science, Universiti Malaya, Kuala Lumpur, Malaysia., Awang K; Department of Chemistry, Faculty of Science, Universiti Malaya, Kuala Lumpur, Malaysia.; Centre for Natural Products Research and Drug Discovery (CENAR), Universiti Malaya, Kuala Lumpur, Malaysia., Khaw KY; School of Pharmacy, Monash University Malaysia, Subang Jaya, Selangor, Malaysia., Qi Mak W; School of Pharmacy, Monash University Malaysia, Subang Jaya, Selangor, Malaysia., Tiamas SG; Department of Chemistry, Faculty of Science, Universiti Malaya, Kuala Lumpur, Malaysia., Maulana S; Department of Pharmacy, Faculty of Mathematics and Natural Sciences, Tadulako University, Palu, Indonesia., Zubair MS; Department of Pharmacy, Faculty of Mathematics and Natural Sciences, Tadulako University, Palu, Indonesia., Pudjiastuti P; Department of Pharmaceutical Science, Faculty of Pharmacy, Airlangga University, Surabaya, Indonesia., Hazni H; Centre for Natural Products Research and Drug Discovery (CENAR), Universiti Malaya, Kuala Lumpur, Malaysia., Liew SY; Centre for Natural Products Research and Drug Discovery (CENAR), Universiti Malaya, Kuala Lumpur, Malaysia.; Chemistry Division, Centre for Foundation Studies in Science, Universiti Malaya, Kuala Lumpur, Malaysia., Zahari A; Department of Chemistry, Faculty of Science, Universiti Malaya, Kuala Lumpur, Malaysia.; Centre for Natural Products Research and Drug Discovery (CENAR), Universiti Malaya, Kuala Lumpur, Malaysia. |
| Abstrakt: |
This study investigated the butyrylcholinesterase (BChE) inhibitory activity of harmane ( 1 ), naucledine ( 2 ), and dihydrodeglycocadambine ( 3 ) isolated from fractions F7 and F9 of Ochreinauclea maingayi . Both fractions demonstrated significant inhibition, exceeding 80%, against BChE at 100 µg/mL. Compound 2 , is the most potent inhibitor, exhibiting an IC 50 value of 22.08 µM, followed by 1 and 3 (IC 50 23.96 and 30.32 µM, respectively). Docking studies revealed that 1 and 2 effectively bind to BChE, with binding energies of -51.24 and -57.17 kcal/mol, respectively. Kinetic analysis of 2 indicated mixed-mode inhibition of BChE, with a Ki of 6.08 μM. In the paralysis assay, 1 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 2 with 70.00 ± 1.7% (2.59% reduction) compared with negative standard (DMSO 0.1%) on human amyloid β -protein in a transgenic Caenorhabditis elegans (CL4176) model. |
