Introduction.

This is a study on a possible molecular coupling of eucalyptol with the viral protease Mpro/3CLpro of SARS-CoV-2. The docking required software using the Auto Dock Vina engines and its tools, as well as online servers, so that the most probable conformations were obtained based on the parameters: binding energies, RMSD, dissociation constant, binding efficiency (E.L) of docking.

Objective.

To determine molecular coupling of eucalyptol with the SARS-CoV-2 viral protease Mpro/3CLpro.

Materials and methods.

To perform the molecular docking, online software and servers were used, in each case the parameters of free rotation of all the ligand bonds with conformational freedom, addition of Gasteiger charges to the protein and the ligand, addition of hydrogens to the protein, generation of 100 poses for the ligand and use of the Lamarckian Genetic Algorithm (LGA). The latter was used under the following conditions: 100 GA runs.

Results.

The active site in the SARS Cov-2 protease had a volume of 226 Å3 with the coordinates (-13.5, 11.3, 71.6) and the following active amino acids: Arg 188, His 41, Pro 168, Met 49, Cys 145 , Thr 190, Asp 187, Glu 166, His 164, Tyr 54, Gln 189, Met 165, Leu 167, Gln 192. The amino acids found in the coupling involved in the interaction with eucalyptol were Phe 140, Cys 145, His 163, His 164, Met 165, Glu 166, His 172; where the hydrophobic interaction is very predominant.

Conclusion.

There is a predominance of intermolecular hydrophobic interaction forces in the coupling, since the hydrophobic characteristics of the active site are due to the fact that the majority of the amino acids found in this active site are hydrophobic in nature.

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