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Structural insight into Mycobacterium tuberculosis maltosyl transferase inhibitors: pharmacophore-based virtual screening, docking, and molecular dynamics simulations

Pharmacophore-based virtual screening, subsequent docking, and molecular dynamics (MD) simulations have been done to identify potential inhibitors of maltosyl transferase of Mycobacterium tuberculosis (mtb GlgE). Ligand and structure-based pharmacophore models representing its primary binding site (pbs) and unique secondary binding site 2 (sbs2), respectively, were constructed based on the three dimensional structure of mtb GlgE. These pharmacophore models were further used for screening of ZINC and antituberculosis compounds database (ATD). Virtually screened molecules satisfying Lipinski’s rule of five were then analyzed using docking studies and have identified 23 molecules with better binding affinity than its natural substrate, maltose. Four top scoring ligands from ZINC and ATD that either binds to pbs or sbs2 have been subjected to 10 ns each MD simulations and binding free energy calculations. Results of these studies have confirmed stable protein ligand binding. Results reported in the article are likely to be helpful in antitubercular therapeutic development research.