Molecular Dynamics Study of Triazole Derivative Binding to the Active Site of Imidazole Glycerol Phosphate Dehydratase from Mycobacterium tuberculosis

Abstract

Models of imidazole glycerol phosphate dehydratase from Mycobacterium tuberculosis in complexes with a number of triazole derivatives, which are known to act as inhibitors of the homologous enzyme of plant origin, were constructed. Molecular dynamics studies showed that these compounds are stably bound to the active site of imidazole glycerol phosphate dehydratase from M. tuberculosis. The position and environment of these derivatives in the enzyme active site are described. The results of these studies can be used to modify the triazole derivatives for the design of selective antituberculosis drugs.