Fig 1.
A graphical representation of the study conducted here to find potential phyto-compounds inhibiting West Nile Virus envelope glycoprotein.
Fig 2.
(Ⅰ) The WNV envelope glycoprotein’s (PDB ID: 2HG0) structure, comprising co-crystallized ligands, side chains, water molecules, and hetatm molecules, (Ⅱ) E-glycoprotein’s structure (Chain-A); applying the removal of water molecules, hetatm molecules, and co-crystallized ligands.
Table 1.
Compounds identification according to PubChem CID, name, and docking value of the top three compounds, as well as Favipiravir (control), with therapeutic uses.
Table 2.
Highlighting the amino acid residues associated with H-bonds, polar bonds, and hydrophobic bonds that form between the target protein and selected three compounds, as well as the control.
Fig 3.
The relationship between the WNV’s E glycoprotein (2HG0) and selected three compounds in 3D and 2D formats, with compounds (A) CID: 359, (B) CID: 9064, (C) CID: 25310, and (D) CID: 492405 in the protein’s active pocket.
Fig 4.
The bar diagram shows MM-GBSA of the compounds CID: 359, 9064, 25310, and the control 492405 demonstrating negative binding free energies.
Table 3.
List of Pk characteristics of three lead compounds with the control (Favipiravir).
Table 4.
List of toxicity characteristics of three lead compounds with the control (Favipiravir).
Fig 5.
The apoprotein’s RMSD, RMSF, Rg, and SASA values are displayed complexed with the three lead compounds and control chosen and extracted from 100 ns MD trajectory complex system’s C
α atoms.
Fig 6.
The bar charts display the P-L interactions determined during the 100 ns simulation period.
In this figure, the 2HG0 protein of the WNV shows interaction with CID: 359 (A), 9064 (B), 25310 (C), and 492405 (control) (D).
Fig 7.
The interaction profiles between the ligand and the apoprotein are presented using the ligand-apoprotein detailed schematic diagram where CID: 359 (A), 9064 (B), 25310 (C), and 492405 (control) (D) illustrate the conformational isomerism of the ligands binding to wild type protein.
Fig 8.
Reflecting the number of H-bonds established by the four selected compounds with the target macromolecule during the 100 ns MD simulation period.
The ordinate of the Y-axis represents the number of hydrogen bonds in the P-L complex, while the ordinate of the X-axis represents time in ns. The colors orange, grey, yellow, and red symbolize CID: 359, 9064, 25310, and 492405 (control), correspondingly.
Fig 9.
Eigenvalue versus proportion of variance in Principal Component Analysis, depicted across three unique panels representing different areas.
Here, (A) CID: 25310, (B) CID: 9064, (C) CID: 359, (D) CID: 492405 (control), and (E) Apoprotein (2HG0) are referenced.
Fig 10.
A comprehensive dynamic cross-correlation map where black indicates positive residue correlations and sea green denotes negative residue correlations.
In this context, (A) CID: 359, (B) CID: 9064, (C) CID: 25310, (D) CID: 492405 (control), and (E) Apoprotein (2HG0) are referenced.