Infection with Giardia lamblia is one of the most common causes of diarrhea worldwide. Fructose1,6-bisphosphate aldolase class II, a key enzyme in the glycolytic pathway of this parasite, plays a crucial role in its energy production. Given the enzyme's importance for parasite survival, its inhibition could offer a novel approach to treating giardiasis. In the present study, we employed molecular docking methods to evaluate the potential of compounds from Origanum vulgare L. to 318 inhibit the Giardia lamblia fructose-1,6-bisphosphate aldolase class II enzyme. Compounds from the plant were extracted from the Lotus and NPASS databases, and their three-dimensional structures were stored in sdf format using the PubChem database. The three-dimensional structure of the enzyme was retrieved from the PDB database (PDB ID: 3GAY) and saved in pdb format. Molecular docking was performed using PyRx software.The results indicated that two compounds, Apigetrin and Taxifolin, demonstrated the highest binding energies (−9.2 and −8.8 kcal/mol, respectively) compared to the control compound Phosphoglycolohydroxamic Acid, which had a binding energy of −6.1 kcal/mol. These compounds showed significant potential to inhibit enzyme activity, thereby halting parasite growth.Preliminary pharmacokinetic and toxicity assessments suggested that these compounds exhibit minimal side effects and toxicity. Therefore, while the findings of this study are promising, further in vitro and in vivo research is required to confirm these results
