Structural and Binding Analysis of IMB-XMA0038 Targeting MtASADH in Mycobacterium tuberculosis: A Molecular Docking and Dynamics Approach

Tuberculosis, caused by Mycobacterium tuberculosis (Mtb), remains one of the major global health problems requiring novel therapeutic approaches. The MtASADH (aspartate-semialdehyde dehydrogenase) enzyme in Mtb is a potential therapeutic target due to its role in bacterial essential amino acid biosynthesis. This study aims to explore the binding mechanism of compound IMB-XMA0038 on MtASADH receptor through in silico approach. The molecular docking method was used to predict the optimal binding position, affinity, and molecular interactions between IMB-XMA0038 and MtASADH. Results showed that IMB-XMA0038 strongly interacted with the active site of MtASADH through hydrogen bonding and significant hydrophobic interactions, exhibiting high binding affinity. In addition, molecular dynamics simulations were performed to evaluate the stability of the complex under physiological conditions, which showed that the IMB-XMA0038-MtASADH complex has good structural stability. This study provides mechanistic insights into the potential of IMB-XMA0038 as a MtASADH inhibitor and supports its development as a novel anti-TB agent. This in silico approach may facilitate further design of more efficient and selective compounds against Mtb.