Interactions of Ozone-Functionalized Activated Charcoal with SARS-Cov-2 Proteases Using Molecular Docking and Dynamics.

The high contamination by the SARS-Cov-2 virus has led to the search for ways to minimize contagion. Masks are used as part of a strategy of measures to suppress transmission and save lives. However, they are not sufficient to provide an adequate level of protection against COVID-19. Activated charcoal has an efficient antibacterial action, adsorption and low cost. Here, the interaction between two molecules of activated carbon was analyzed, interacting with two structures of the SARS-Cov-2, through docking and molecular dynamics using the platforms Autodock Vina 4.2.6, Gaussian 09 and Amber 16. As a result, the complexes from ozone-functionalized coal to viral structures happen mainly through hydrophobic interactions at the binding site of each receptor. The values of the mean square deviations of the two systems formed by ligands/receptors and showed better stability. The results of Gibbs free energy showed a better interaction between proteins and functionalized charcoal, with △Gtotal values of -48.530 and -38.882 kcal/mol. Thus, the set formed by combinations of proteins with functionalized activated carbon tends to more efficiently adsorb the protein components of the coronavirus to the pores of the activated carbon with ozone during filtration.

Interactions Between Remdesivir, Ribavirin, Favipiravir, Galidesivir, Hydroxychloroquine and Chloroquine with Fragment Molecular of the COVID-19 Main Protease with Inhibitor N3 Complex (PDB ID:6LU7) Using Molecular Docking.

We started a study on the molecular docking of six potential pharmacologically active inhibitors compounds that can be used clinically against the COVID-19 virus, in this case, remdesivir, ribavirin, favipiravir, galidesivir, hydroxychloroquine and chloroquine interacting with the main COVID-19 protease in complex with a COVID-19 N3 protease inhibitor. The highest values of affinity energy found in order from highest to lowest were chloroquine (CHL), hydroxychloroquine (HYC), favipiravir (FAV), galidesivir (GAL), remdesivir (REM) and ribavirin (RIB). The possible formation of hydrogen bonds, associations through London forces and permanent electric dipole were analyzed. The values of affinity energy obtained for the hydroxychloroquine ligands was -9.9 kcal/mol and for the chloroquine of -10.8 kcal/mol which indicate that the coupling contributes to an effective improvement of the affinity energies with the protease. Indicating that, the position chosen to make the substitutions may be a pharmacophoric group, and cause changes in the protease.