In-Silico Study of Ethambutol and Its Derivatives On 7nt7 Receptor for Anti-Tuberculosis Activity
Year: 2025
Type: article
Abstract: The present study was undertaken to evaluate the binding potential and molecular interactions of ethambutol, an established first-line anti-tubercular drug, using molecular docking techniques. Tuberculosis (TB) remains a major global health challenge, particularly with the emergence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) strains of Mycobacterium tuberculosis. Ethambutol, known to inhibit arabinosyl transferases involved in cell wall biosynthesis, was evaluated in this project for its interaction with the enzyme decaprenyl phosphoryl-β-D-ribose 2′-epimerase (DprE1), which plays a critical role in the synthesis of the mycobacterial cell wall. Using Auto Dock software, the docking analysis revealed that ethambutol binds efficiently within the active site of the DprE1 protein, forming multiple interactions, including hydrogen bonds with key amino acid residues such as Tyr60, Gly117, and His132. The binding energy was calculated to be -5.2 kcal/mol, indicating a moderately strong and stable interaction between the ligand and the target protein. Such interactions may inhibit the enzymatic activity of DprE1, thereby supporting the pharmacological action of ethambutol in disrupting the integrity of the bacterial cell wall. The molecular docking results obtained from this study align with the known pharmacodynamic properties of ethambutol and provide computational validation of its mechanism of action. Furthermore, these findings highlight the importance of target-based drug discovery and the relevance of molecular docking studies in understanding drug-target interactions at the molecular level. In addition to enhancing our understanding of ethambutol’s mode of action, this study also demonstrates the utility of molecular modeling tools in modern pharmaceutical research. Such computational techniques can be effectively employed to screen potential drug candidates, predict their binding affinities, and design new analogs with improved efficacy and specificity. To conclude, the docking study of ethambutol with the DprE1 protein has successfully illustrated a strong theoretical basis for its inhibitory action, thereby reinforcing its therapeutic relevance. This project lays a foundation for further in vitro and in vivo studies, which are essential to validate these findings and to explore possible structural modifications of ethambutol or the design of new anti-TB agents with similar or enhanced activity. As the burden of tuberculosis continues to threaten global health, studies like this contribute to the ongoing efforts in anti- tubercular drug research and development.
Author: Dr. Dinesh Kawade*, Shriya Bagh, Shikha Shahu, Yashika Bhattad Sejal Kshirsagar
Language: English
Subfield: Computational Theory and Mathematics
Field: Computer Science
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W6893383191
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