Philippine Journal of Science
151 (2): 545-561, April 2022
ISSN 0031 – 7683
Date Received: 10 Oct 2021

Cholinesterase Inhibitory Activities and In Silico
Docking Studies of Blumeatin Isolated
from Blumea balsamifera L. DC.

Rosemarie Elloisa P. Acero* and Evangeline C. Amor

Terrestrial Natural Products Laboratory, Institute of Chemistry
University of the Philippines Diliman, Quezon City 1100 Philippines

*Corresponding author: rpacero@up.edu.ph

 

[Download]
Acero RE, Amor E. 2022. Cholinesterase Inhibitory Activities and In Silico Docking Studies of Blumeatin
Isolated from Blumea balsamifera L. DC. Philipp J Sci 151(2): 545–561. https://doi.org/10.56899/151.02.01

 

ABSTRACT

Cholinesterase inhibition provides symptomatic treatment for neurodegenerative diseases such as Alzheimer’s disease. Commercially available drugs on the market mostly target acetylcholinesterase. However, evidence suggests that selective inhibition of butyrylcholinesterase may lead to greater efficacy with fewer side effects and slower disease progression. The aim of this research was to isolate a butyrylcholinesterase-selective inhibitor from Blumea balsamifera L. DC. In vitro cholinesterase assays were used to evaluate the inhibitory activity and mechanism of action of blumeatin. Molecular docking studies were performed to support the BuChEselectivity of blumeatin. Blumeatin inhibited BuChE in a concentration-dependent manner, with an IC50 of 136.3 ± 12.6 μM and a selectivity ratio of 1.395 for BuChE over AChE. Additionally, the Ki of blumeatin is 10 times lower in BuChE compared to AChE. Molecular docking studies confirmed the selectivity, as revealed by the tighter hydrogen bonding of blumeatin with the BuChE’s active site. Blumeatin acts as a competitive inhibitor and a noncompetitive inhibitor of BuChE and AChE, respectively. With these results, blumeatin could be a potential lead as a drug treatment for AD because of its butyrylcholinesterase selectivity