The present study aimed to evaluate the inhibitory potential of selected plant-derived compounds against the target protein (PDB ID: 4TZK) through molecular docking analysis. The three-dimensional structure of the protein was retrieved from the RCSB Protein Data Bank and docking simulations were performed using PyRx. A total of ten phytocompounds—Bilobetine, Tetrandrine, Lobenine, Nolatrexed, Sophoraflavanone G, Isoquirigenine, Luteolin, Aloin, Cinchonine, and Licochalcone A—were evaluated, with Isoniazid used as the reference drug. The docking results revealed that all selected compounds exhibited stronger binding affinities than Isoniazid (−5.2 kcal/mol). Among them, Bilobetine demonstrated the highest binding affinity (−10.4 kcal/mol), followed by Tetrandrine and Lobenine (−8.9 kcal/mol). Interaction analysis indicated the involvement of key active-site residues, including TYR-158, PHE-149, MET-199, and ILE-194, through hydrogen bonding, π–π stacking, and hydrophobic interactions. Structure–activity relationship analysis suggested that aromatic ring systems, hydroxyl substitutions, and hydrophobic moieties significantly contribute to enhanced binding stability. Overall, the findings indicate that these phytocompounds possess promising inhibitory potential and warrant further experimental validation for therapeutic development.
Ronak Patadiya1, Sangita Shukla1, Nikunj Patadiya2* (Tue,) studied this question.