Open AccessModeling the interaction of thiozonide and atphase M.tuberculosis by the method of molecular docking
Author(s) -
Б. В. Шилов,
А. С. Смирнов,
А. Yu. Savchenko
Publication year - 2021
Publication title -
biomedicina
Language(s) - English
Resource type - Journals
eISSN - 2713-0428
pISSN - 2074-5982
DOI - 10.33647/2713-0428-17-3e-170-175
Subject(s) - autodock , docking (animal) , protein subunit , in silico , atp synthase , stereochemistry , chemistry , atp hydrolysis , enzyme , binding site , transmembrane domain , transmembrane protein , computational chemistry , biochemistry , atpase , membrane , receptor , medicine , nursing , gene
The mechanism of interaction of a new anti-tuberculosis drug thiosonide with a probable target of M. tuberculosis was studied. According to the data obtained, the most likely target with a thiozonide binding pocket is the subunit of bacterial ATP synthase, an enzyme that plays a key role in the processes of energy exchange in the cell, coupling the reaction of ATP synthesis/hydrolysis with transmembrane proton transfer. Original models of the three subunits of this enzyme (alpha, delta, and epsilon) were built. To simulate docking in silico, the AutoDock program version 4.2 was used, which is included in the MGL Tools version 1.5.6. It was shown that all three subunits have clusters with the minimum binding energies for the thiosinide molecule, and the epsilon subunit has two clusters with equal probabilities of being a thiosinide binding site.