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The present study aimed at studying the potential of methanolic extract of Muntingia calabura bark (MBE) to inhibit acetylcholinesterase (AChE) in vitro
Acetylcholinesterase (AChE) activity was assessed using chicken brain homogenate as the enzyme source. The assay was performed using acetylthiocholine iodide as a chromogenic substrate, and the reaction was monitored kinetically at 412 nm by measuring the rate of substrate hydrolysis.
MBE was found to inhibit the AChE activity with an IC50 value of 78.6 ± 2.3 mg/mL. Analysis of the double reciprocal Lineweaver-Burk plot revealed that the rate of substrate hydrolysis by the brain homogenate was characterized by the Km and Vmax values of 93.7 ± 18.8 mM and 0.145±0.009 (delta OD/min at 412nm), respectively. In the presence of the MBE, we observed Km and Vmax values of 76.5 ± 8.9 (without statistical difference compared to the control) and 0.07 ± 0.007 (delta OD/min at 412 nm, statistically lower than the control), respectively, indicating that the MBE non-competitively inhibits AChE.
The data presented herein suggest that MBE inhibits AChE in vitro. Additional experiments are required to establish oral availability, toxicity, and efficacy in vivo.
Our work demonstrates the potential of MBE to inhibit AChE in vitro and suggests that the extract warrants further exploration for molecular characterization and potential usefulness in mitigating pathologies in animal models of Alzheimer’s disease.
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