In a work similar to the one reported here, Vipul Kumar and colleagues used autodock vina to determine that both, FA and its metabolites tetrahydrofolic acid and 5-methyltetraydrofolic acid, have high affinity to bind as ligand to ACE2 and therefore, they assumed that these metabolites can prevent the RBD-ACE2 binding. As in the other proposals previously cited in this subsection , they draw their conclusions based solely on the binding energy of the ligand with the protein and the stability (Root-Mean-Square Deviation) of this binding. Even if the binding energy and stability ligand-protein are high, this does not mean that the ligand modifies the functions of the protein, either by increasing or decreasing its biological activity in a competitive or non-competitive way. For example, glucose has a high affinity to bind as a ligand to hemoglobin; however, although glucose can make some conformational alterations in the structure of hemoglobin , it does not play a significant role in the oxygen affinity pattern of diabetics at the concentrations normally found in vivo . For this reason, this research employed autodock vina not only to find the highest affinity poses of FA and some of its metabolites at the ACE2 receptor, but we also used these poses to build an ACE2-metabolite complex to simulate the interactions between RBD and ACE2 in different scenarios using MD. These interactions are further described in the following sections.