Pharmaceutica Analytica Acta

Abstrait

Similarity in the Amino Acid Sequences of Mycobacterium tuberculosis Protein Targets Involved in Binding Sites of Docking with Thiacetazone

Mafakheri M and Sardari S

Although according to WHO document, between 1990 and 2015, both TB mortality and its incidence has been fallen over 47% worldwide, the spread of multidrug-resistant strains of Mycobacterium tuberculosis reveals clearly that the efforts to find new drugs should not be stopped and the pathogenic microorganisms develop resistance. More extended knowledge about existing drugs is critical to design new and more effective medicines. In this study, we report the amino acid sequences involved in binding sites of 70 M. tuberculosis protein targets’ docked with Thiacetazone (TAC), one of the extensively used antitubercular drug that is used in combination with other antitubercular agents to break multi-drug resistant TB. Categorization of protein targets was performed on the basis of the free energy of binding for the docked compounds. Comparison of the binding sites with the aim of ClustalW application indicated huge similarities in their amino acid sequences among target complexes.