The α-hemolysin protein forms a β-barrel structure, creating a pore on the plasma membrane's surface, facilitating its toxic activity. This study aimed to investigate the potential of small molecules to block or close this pore, thus inhibiting the toxin's function. The docking of various ligands to the α-hemolysin protein was performed, and the results are presented in Figure . Analysis of the 2D interaction profiles between the protein and the ligands revealed that Ligand III and Ligand IV formed significantly stronger interactions with the protein than Ligand I and Ligand II. These stronger interactions are attributed to more extensive hydrogen bonding and hydrophobic contacts within the binding pocket of the β-barrel. Moreover, Ligand III and Ligand IV exhibited larger binding surfaces, which could contribute to more effective pore occlusion.