Background: Treatment of the COVID19 pandemic requires drug development. Boron-containing compounds are attractive chemical agents, some of them act as proteases inhibitors.
Objective: The present study explores the role of boronic moieties in molecules interacting on the binding site of the SARS-CoV-2 main protease.
Methods: Conventional docking procedure was applied by assaying boron-free and boron-containing compounds on the recently reported crystal structure of SARS-CoV-2 main protease (PDB code: 6LU7). The set of 150 ligands includes bortezomib and inhibitors of coronavirus proteases.
Results: Most of the tested compounds share contact with key residues and poses on the cleavage pocket. Those compounds with a boron atom in its structure were often estimated with higher affinity than boron-free analogues.
Conclusion: Interactions and the affinity of boron-containing peptidomimetics strongly suggest boron-moieties increases affinity on the main protease, as it should be tested by in vitro assays. A Bis-boron-containing compound previously tested as active on SARS-virus protease and bortezomib were identified as potent ligands. These advances may be relevant for drug designing, in addition as to the suggestion of testing available boron-containing drugs in patients with COVID19 infection.