In contrast, in the scenario A, the RBD and ACE2 move further away at 5 ns, and then they move closer. At 75 ns, they definitely separate, the complex is broken and the LJ-SR energy becomes zero. The hydrogen bonds also disappear, which leads to the conclusion that the RBD cannot form a stable complex with the ACE2. Therefore, the Wild type SARS-CoV-2 virus could not stay attached to the ACE2 receptor and consequently could not initiate host cell infection. FIG. : Minimum distance between RBD and ACE2 during the simulation trajectory. It can be seen that in the control (Wild type), B (Beta + DHF) and C (Delta + DHF) cases the RBD and ACE2 approach until they form a stable complex that remains interacting without moving away from each other during the entire trajectory. In contrast, it can be observed that in the A (Wild + DHF) case of intervention the RBD and the ACE2 move away from each other at 75 ns. FIG. : LJ-SR interaction energy between RBD and ACE2 during the simulation trajectory. It can be seen that in the control (Wild type) and B (Beta + DHF) and C (Delta + DHF) cases, the LJ-SR energy is the lowest, which can be interpreted as a binding with higher affinity. In contrast, in the A intervention (Wild + DHF) the binding energy is higher (lower affinity). In the case of control (Wild type) and intervention B (Beta + DHF) and C (Delta + DHF), it can be observed that during the trajectory the greatest number of hydrogen bonds is maintained. In contrast, it can be observed that in the A scenery (Wild + DHF) at 75 ns there are zero hydrogen bonds and this is maintained for the rest of the trajectory.