Fig 1.
The TLR4-2-Bromoergocryptine Mesylatemesylate complex 3D structure, as well as the 3D and 2D interaction diagram.
The left panel shows a 2D interaction plot of 2-Bromoergocryptine Mesylate and TLR4. The Pi-Alkyl bond is shown by pink dashed lines, whereas residues wrapped inside a light green sphere are thought to be involved in Van der Waals interactions. The binding cavity of the 2-Bromoergocryptine Mesylate molecule is shown in the center panel of TLR4, while the right panel shows a zoomed-out binding pocket with amino acid residues surrounding the molecule.
Table 1.
10 ligands with the most auspicious binding affinity with TLR4 was calculated by molecular docking analysis.
Fig 2.
MD simulation trajectory analysis of Root Mean Square Divisions (RMSD) of Bromocriptinemesylate bound with TLR4 at 150 ns time frame.
Fig 3.
MD simulation trajectory analysis of hydrogen bonding of 2-Bromoergocryptine Mesylatebound with TLR4 at 150 ns time frame.
Fig 4.
MD simulation trajectory investigation of 2-Bromoergocryptine Mesylateassociated with TLR4 RMSF at 150 ns time frame shown.
Fig 5.
MD simulation trajectory analysis of Radius of Gyration (RoG) of 2-Bromoergocryptine Mesylatebound with TLR4 at 150 ns time frame displayed.
Fig 6.
Protein-ligand contact histogram (H-bonds, hydrophobic, ionic, water bridges) of TLR4 and 2-Bromoergocryptine Mesylate.
Fig 7.
Secondary structure element distribution by residue index throughout the protein structure.
Red indicates alpha helices, and blue indicate beta-strands of TLR4 and 2-Bromoergocryptine Mesylate.