Egyptian Journal of Chest Disease and Tuberculosis (Jan 2021)
Identification and evaluation of Calotropis procera phytocompounds against novel protein PE_PGRS 16 from Mycobacterium tuberculosis H37Rv
Abstract
The authors are currently dealing with the highest incidence of tuberculosis, where every third person in the world is experiencing the latent condition of the disease. The affected ratio is not limited to any age group, and therefore, the development of new drug or vaccine is the need of the hour. The use of medicinal plants in curing disease is a novel and significant area of interest. The PE_PGRS 16 has putative aspartic proteinase domain, which reveals the characteristic of pepsin-fold and is recognized as a surface antigen; therefore, it would be an important target for drug design. The structure of PE_PGRS 16 was obtained from PDB databank and the phytocompounds of Calotropis procera were obtained from gas chromatography–mass spectrometry analysis. PyRx tool and AutoDock Vina were used to prepared dock file and docking analysis, respectively. The compounds were selected based on docking score, and selected compounds were further checked by absorption, distribution, metabolism, and excretion (ADME) properties to conclude a list of safe and effective drugs. Visualization and analysis of interaction was done by Discovery Studio Visualizer. Screened phytocompounds against the PE_PGRS 16 accurately fitted within the active sites. The structural analysis suggested the binding to residues Asp46, Thr47, and Gly48 short sequence motif D(T/S)G 1, Asp199, Ser200, and Gly201 D(T/S)G 2 with the compound. These residues are important for protein activity, and therefore, drug binding at these residues may hamper protein’s activity. l-rhamnose and ferulic acid closely interacted with active site residue of PE_PGRS 16, and therefore, it is hypothesized that these compounds are the putative target of the protein activity, which enhance bacterial pathogenesis and survival.
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