Alpha-hemolysin (α-toxin), a pore-forming toxin that may lyse various host cells, is a virulence factor that makes Staphylococcus aureus a clinically significant pathogen. One intriguing approach to creating new antimicrobial medicines may be to interfere with this toxin's interaction with host targets. Using molecular docking simulations, this work seeks to determine whether tiny compounds can inhibit S. aureus's alpha-hemolysin. Several processes, such as synthesizing anti-inflammatory compounds and using host components for iron acquisition, help S. aureus survive and remain in the host. One of this virus's most notable virulence factors is alpha-hemolysin, commonly referred to as α-toxin, which can lyse red blood cells and affect a variety of cells with nuclei. Furthermore, since the removal of these enzymes reduced the bacterial burden during infection, it has been proposed that S. aureus's development of nucleases functions as an evasion mechanism. We conducted a structure-based virtual screening campaign to find tiny compounds that can interfere with alpha-hemolysin's ability to engage with its host targets.