Druggable proteins of Alistipes reveal promising antimicrobial targets against chronic intestinal inflammation

A set of 39 potential proteins was drastically reduced to only two targets after sequential data mining. The 3D structures of the selected targets (<i>LpxA</i> and <i>KdsB</i>) revealed good druggability scores. The top hits (ZINC85530940, ZINC05161112, ZINC95911713, and ZINC05566415) for both targets showed maximum H-bond interactions. The RMSD and RMSF values exhibited compactness with minimum fluctuation in ligand-bound complexes. The β-factor of ZINC05161112 at 327th residue and 352nd residue exhibited higher thermal instability, consistent with the RMSF results. The globularity of the complexes and apo structures remained consistent, whereas the <i>LpxA</i> complexes exhibited lower solvent-accessible surface area. For the <i>KdsB</i>, the surface area for ZINC5566415 increased significantly, with a steep decrease for ZINC95911713, establishing rather stable protein-ligand complexes. The results highlight the importance of identifying novel inhibitors and therapeutic targets. They are crucial for establishing better treatment regimes for human health and to aid in controlling the pathogenicity of <i>Alistipes</i> species.