Fig 1.
A stepwise workflow was employed to exploring Dolichos lablab compounds as potential inhibitors for Fusion (F) protein of human metapneumovirus (HMPV).
Table 1.
Binding affinity between Fusion (F) protein of HMPV and Dolichos Lablab (Lead compounds).
Fig 2.
Docking poses of Brassinolide, Quercetin, and 2’-Hydroxygenistein with Fusion (F) protein of HMPV.
Fig 3.
Non-bonding interactions between the fusion protein of HMPV and Brassinolide, Quercetin, 2’-Hydroxygenistein, and Ribavirin.
Table 2.
Drug-likeness properties of lead compounds using SwissADME.
Table 3.
Pharmacokinetics properties of selected lead five compounds.
Table 4.
Predicted physicochemical properties related to drug-likeness of lead compounds.
Fig 4.
Chemical scaffold of Brassinolide, Quercetin, 2’-Hydroxygenistein, and Ribavirin.
Fig 5.
Molecular dynamics simulation of three selected protein–ligand complexes and a ribavirin compound with a 100 ns runtime.
(a) Root Mean Square Deviation (RMSD); (b) Root Mean Square Fluctuation (RMSF); (c) Radius of Gyration (Rg); and (d) Solvent accessible surface area (SASA).
Fig 6.
Protein–ligand interactions through various types of bonds at 100 ns simulation running time.
The selected compounds Brassinolide, Quercetin, 2’-Hydroxygenistein and ribavirin complexed with the target protein were marked as a, b, c, and d respectively.
Fig 7.
Binding free energy values for the top three protein–ligand complexes and one ribavirin complex obtained from the PRODIGY server have been visualized in the graph.