With the advancement of the Covid-19 pandemic, this work aims to find molecules that can inhibit the attraction between the Spike proteins of the SARS-COV-2 virus and human ACE2. The results of molecular docking positioned four molecules at the interaction site Tyr-491(Spike)-Glu-37(ACE2) and one at the site Gly-488(Spike)-Lys-353(ACE2). The QTAIM and IQA data showed that the 1629 molecule had a significant inhibitory effect on the Gly488-Ly353 site, decreasing the Laplacian of the electronic density of the BCP O4 -N10 . The molecule 2542 showed an inhibitory effect in two regions of interaction of the Tyr491-Glu37 site, acting on the BCPs H30-H33 and O8-H31 while the ligand 2600, in conformation 26, presented a similar effect only on the BCP O8-H31 of that same interactive site. Thus, the data suggest laboratory tests of a combination of molecules that can act at two sites of interaction simultaneously, using the combination of 1629/2542 and 1629/2600 ligands.
Professor Sergio Henrique Dias Marques Faria received a bachelor’s degree in Chemistry at the State University of Campinas (UNICAMP-BRAZIL). Faria did a Master and Doctorate in Theoretical Chemistry applied to Spectroscopy (UNICAMP). As Titular Professor at Universidade Paulista, Faria worked on the application of Molecular Docking calculations combined with electronic density (DFT) to quantify the interaction of antineoplastic agents with DNA fragments to clarify chemical mechanisms and new drug developments. These methods were used to develop drugs to inhibit SARS-COV-2 infection. Currently, Faria also works as a Postdoctoral Researcher at the University of São Paulo with atomic partition models for the study of singlet oxygen formation through photosensitizers.