Elucidating isoniazid resistance in M ycobacterium tuberculosis using molecular docking approach.

Unissa, A.N.; Hassan, S.; Selvakumar, S.

International Journal of Pharma and Bio Sciences; 2012; 3; 314-326.

Abstract: I soniazid, an important drug in the anti-tuberculosis therapy, the enzyme catalase-peroxidase (KatG) plays a key role in activating isoniazid (INH). Mutation in katG gene is a major mechanism of INH resistance in M. tuberculosis . Several derivatives of INH show activity against TB and multi-drug resistant TB. With the aim of finding new compounds, in this study, the derivatives of INH were docked directly with wild type and the mutated models of KatG from M. tuberculosis using in-silico approaches. Docking results suggests that compounds-10, 12 and 13 were the high scoring derivatives of INH to bind with mutants of KatG. These models represent the first in-silico evidence for the binding interaction of KatG and its mutants with INH derivatives. The models may provide useful insights for designing new anti-TB agents in order to overcome the resistance developed with INH.

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