Structure-Based Study of Piperine Phytochemical Against InhA Protein of Tuberculosis

Author(s)	Ms. Rani Bhanudas Sathe, Ms. Syeda Afifa
Country	India
Abstract	The docking analysis demonstrated that piperine exhibited favorable binding affinity toward the InhA protein, indicating the formation of a stable ligand–protein complex. The interaction study revealed significant hydrophobic interactions along with hydrogen bond formation between piperine and important amino acid residues present in the active site region of the protein. The negative docking score suggested strong intermolecular interactions and good binding stability, thereby supporting the inhibitory potential of piperine against the selected target protein. Visualization of 2D and 3D ligand interaction profiles further confirmed the effective accommodation of piperine within the active binding cavity of InhA. conclusion, the present molecular docking study suggests that piperine possesses promising inhibitory activity against the InhA protein of Mycobacterium tuberculosis. The observed binding affinity and interaction profile indicate that piperine may serve as a potential lead compound for the development of novel anti-tubercular agents. However, further in vitro and in vivo studies are required to validate its biological efficacy, safety, and therapeutic potential in tuberculosis treatment.
Keywords	piperine phytochemical, molecular docking, targe protein (InhA), Anti- tubercular activity
Field	Medical / Pharmacy
Published In	Volume 17, Issue 5, May 2026
Published On	2026-05-23

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