In this work, we used molecular docking simulations with various small compounds to investigate the suppression of Staphylococcus aureus alpha-hemolysin toxin. According to our research, Ligands III and IV exhibited the highest binding contacts with the alpha-hemolysin protein's pore-forming region. This was demonstrated by their high binding affinities and extensive hydrophobic and hydrogen bonding interactions. These ligands showed promise in efficiently inhibiting the transmembrane pore's development, which would stop cellular lysis and lessen the pathogenicity of the toxin. This work establishes the groundwork for creating targeted therapy treatments against Staphylococcal infections by concentrating on pore inhibition as a promising therapeutic approach. Future research should focus on in vitro and in vivo validation to verify these ligands' safety and effectiveness as therapeutic agents and molecular dynamics simulations to evaluate their stability in a dynamic cellular context.