The discovery of anti-tuberculosis agents is crucial for effective tuberculosis therapy. The present strategy for new drug development is directed towards identifying essential enzyme systems in the bacteria and developing potent molecules to inhibit them. The aim of this study was to study the inhibition of a peptide deformylase of Mycobacterium tuberculosis using molecular docking FlexX. This study highlighted the actinonin as the better inhibitor of the enzyme. The study of the modelling realized on this inhibitor show that the binding energy can be decreased in a significant way by a judicious choice of fragments to be substitutes. Replacement of the pentyl group in position R1 by a cyclopentylmethyl, the dimethyl-propyl group in position R2 by a pyrrolidine and the hydroxymethyl pyrrolidin in position R3, by hydroxyphenyl group decreases the energy of interaction of 8 units. The study of the pharmacokinetic properties of this proposed molecule shows that they join perfectly the margin of the criteria imposed by the rule of Lipinski. The results of the present study are reported herein so that researchers, who are having required laboratory facilities for synthesizing drugs, can utilize findings of this study for developing new drugs against Mycobacterium tuberculosis with better efficacy.
