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May 13, 2026

Synthesis, DFT, and Molecular Docking Studies of Substituted Benzimidazole Scaffolds as Potential Antimicrobial and Antitubercular Agents

Key Points

To explore benzimidazole derivatives as potential antimicrobial and antitubercular agents in light of rising antibiotic resistance.
Synthesized and characterized benzimidazole hybrids using FTIR, NMR, and mass spectrometry.
Screened antimicrobial potential against ESKAPE Panel, NTMs, and M. tuberculosis H37Rv27294.
Conducted molecular docking studies on S. aureus tyrosyl-tRNA synthetase and KasA enzyme.
Compound 3c demonstrated significant antibacterial activity with MIC values of 1.0 µg/mL against E. faecalis and 0.5 µg/mL against S. aureus.
Compound 3c showed an MIC of 8.0 µg/mL against M. tuberculosis H37Rv27294.
Molecular docking revealed 3c had a binding energy of -9.85 kcal/mol with S. aureus tyrosyl-tRNA synthetase.

Abstract

ABSTRACT The rise in antibiotic resistance has become a global health challenge as many of the existing drugs are increasingly ineffective in combating infectious diseases. The benzimidazole hybrids have emerged as new class of antimicrobial agents and as a result there is considerable attention in the design and synthesis of new benzimidazole derivatives. This study describes the synthesis of benzimidazole hybrids and their characterization by FTIR, NMR ( 1 H and 13 C) and mass spectral data. The compounds were screened for antimicrobial potential against the ESKAPE Panel, NTMs, and M. tuberculosis H37Rv27294. Among the tested compounds, 2,4‐dibromo‐6‐(5‐nitro‐1H‐benzodimidazol‐2‐yl)phenol ( 3c ) demonstrated significant potential to inhibit E. faecalis and S. aureus with an MIC values of 1.0 and 0.5 µg/mL, respectively. Compound (3c ) also exhibited immense potential against M. tuberculosis H37Rv27294 with the MIC, 8.0 µg/mL Molecular docking studies on S. aureus tyrosyl‐tRNA synthetase protein, which is essential for bacterial survival, revealed that among all the compounds screened, compound ( 3c ) possesses better affinity with a binding energy of −9.85 kcal/mol. Further, investigation of 3c targeting KasA (β‐ketoacyl‐acyl carrier protein), a crucial enzyme in the mycobacterial FAS‐II pathway, showed a binding energy of −7.1 kcal/mol suggesting 3c could be explore as a promising lead molecule.

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