Molecular Docking and Dynamics Simulation Analysis of Daidzein 4′-Sulfate Binding To Β-Ketoacyl-[Acyl Carrier Protein] Synthase III (FABH) Of Escherichia Coli: Insights into Binding Mechanism and Stability

The study explores the potential of diadzein 4’-sulfate as lead compound targeting fatty acid biosynthesis particularly drug resistant strains of E.coli. Molecular docking was performed using Autodock 4.2.6 to evaluate the binding affinity and the pose of the ligand within the target protein FabH. Further stability and structural behaviour of diadzein 4’-sulfate-FabH complex was studied by MD simulation. Following energy minimization, both the protein and the ligand adopted stable and energetically favourable confirmations. Binding site prediction using P2Rank identified the top ranked pocket with a score of 23.17 and binding probability of 0.87. The molecular interaction profile of diadzein 4’-sulfate with FabH was characterized using Discovery Studio revealing a well-defined and stable binding mode with the predicted binding site Favourable binding characteristics and dynamic stability of the protein and ligand highlights its potential as a natural product for development of FabH targeting antibacterial drug.