BRAZ, Luana Camilla Cordeiro.; BRAZ, Liliane Karine Cordeiro.; NOBREGA, Franklin Ferreira de Farias.; MAIA, Rafael Trindade.
Résumé:
In late 2019, a new coronavirus (SARS-CoV-2) emerged in China causing the
biggest viral pandemic in recent times. The inexistence of speciic medications led to an incessant
race for the repositioning of drugs in the scientiic world, to identify promising molecules for the
treatment of COVID-19. NSP9 is a replicase that is associated with viral replication of SARSCoV-2 and therefore represents an important target for inhibitor compounds. Terpinen-4-ol is a
monoterpene with numerous pharmacological properties, including antimicrobial and antiviral
activities. The present study aimed to perform molecular docking simulations between NSP9
and (-)-terpinen-4-ol. The molecules were obtained from a public database (PDB and ZINC).
The Autodocktools 1.5.6 program was used for the docking simulations, while the interaction
analysis and visual analysis of the complexes were performed using the DS-Discovery Studio
program. The binding energies obtained had negative values ranging from -4.39 to -4.19
kcal/mol. The monoterpene interacted with 8 amino acids from the enzyme’s catalytic site,
most of which were hydrophobic. A hydrogen bond was formed between the ARG40 and
the hydroxyl group of the ligand. The other interactions were represented by alkyl and pialkyl bonds promoted by three amino acids and van der Walls interactions with four other
amino acids. These results indicate an afinity between the ligand and the active site of the
enzyme. Terpinen-4-ol is an interesting candidate for in vitro and in vivo assays to determine
the potential for viral inhibition of SARS-CoV-2.
