Figure 5
From: Cardol triene inhibits dengue infectivity by targeting kl loops and preventing envelope fusion
Molecular docking and MD simulation. (A) Structural comparison between DENV and ZIKV E proteins at kl loops. (B) Molecular docking of phenolic lipids and β-OG at kl hydrophobic pockets of DENV E dimer. (C–E) Structural dynamics of cardol triene to K and K’ sites of DENV E dimers. (C) Total binding free energy (ΔG bind) of cardol triene and K and K’ sites at 60–100 ns-trajectories at 297 and 310 Kelvin were compared with FN5Y at 297 K using SIE method. (D) Total binding free energy (ΔG bind) of cardol triene and K and K’ sites at 200–300 ns-trajectories at 297 and 310 Kelvin generated from SIE, MM-GBSA, MM-PBSA, and QM/MM-GBSA were compared. (E) Binding regions and residues were revealed as follows; 48–54 (T48, E49, A50, P53), 128–135 (K128, V130, L135), 191–207 (M196, L198, Q200, W206, L207), and 270–281 (I270, and L277).
