Abstract
The aim of the present docking study was to explore the putative role of
boronic moieties in molecules interacting on the binding site of the SARS-CoV-2 main protease. The methodology was based on
the conventional docking procedure by means of AutoDock software by assaying
boron-free and boron-containing compounds on the recent reported crystal
structure of SARS-CoV-2 main protease (PDB
code: 6LU7). The most of
tested compounds share contact with key residues and poses on the cleavage
pocket. Those compounds with a boron atom in its structure often were estimated
with higher affinity than boron-free analogues. Interactions and affinity of boron-containing
peptidomimetics on the binding site let us to propose the potent inhibition of
these compounds on targeted protease. These advances may be relevant for drug
designing, but also to suggest the testing of available boron-containing drugs
in patients with severe symptoms of COVID19 infection.