Molecular Docking Study of the Inhibition Influenza B Virus by Some Selected Carboxylic Acids
نویسندگان
1 Department of Pure and Applied Chemistry, University of Maiduguri
2 Department of Pure and Applied Chemistry, University of Maiduguri
3 Department of Pure and Applied Chemistry, University of Maiduguri
4 Department of Pure and Applied Chemistry, University of Maiduguri
5 Department of Pure and Applied Chemistry, University of Maiduguri
6 Department of Pure and Applied Chemistry, University of Maiduguri
doi
10.22036/org.chem.2023.401924.1288چکیده
Influenza viruses are major human pathogens accountable for respiratory diseases affecting millions of people worldwide and characterized by high morbidity and significant mortality. Influenza infections can be controlled by vaccination and antiviral drugs. A molecular docking study was conducted to compute the scoring function and research protein-ligand interactions in predicting the binding affinity and biochemical activity of some carboxylic acids compounds (6-acetamido-5-amino-1-(2-ethylbutanoyl)-1,4,5,6-tetrahydropyridazine-3-carboxylic acid, 6-acetamido-5-((diaminomethylene)amino)-1-(2-ethylbutanoyl)-1,4,5,6-tetrahydropyridazine-3-carboxylic acid, 6-acetamido-5-amino-1-(2-ethylbutanoyl)-1,4,5,6-tetrahydropyridazine-3-carboxylic acid). The docking results shows that THP3b (5-amino-1-(2ethylbutanoyl)-6-((flurocarbonyl)amino)-1,4,5,6-tetrahydropyridazine-3-carboxylic acid) has the lowest binding affinity with a score of -19.244kcal/mol but in turn has the best binding affinity when compared to all other compounds. The result shows that the designed ligand THP3b is very stable and maintain its firm position within the binding pocket of 1INF receptor, indicating that the complex is stable under the varying conditions and THP3b can be used as a drug candidate for treating influenza B Virus.
