Abstract
The genus Plasmodium falciparum, known to be the most lethal form of malaria, is developing resistance to existing treatments, urging the need for new therapeutic targets. In this study, we focused on the P-type ATPase proteins, identifying PfATP4 as a potential drug target for new antimalarial treatments. Studies have shown that Spiroindolones are promising inhibitors for this protein. Using the Molecular Operating Environment (MOE) software, we created a homology model of PfATP4 and located a potential binding site within its transmembrane region. Our computational methods included molecular docking and molecular dynamics (MD) simulations, closely examining hydrogen and hydrophobic interactions between Spiroindolones and PfATP4. Additionally, we conducted a pharmacophore search across different libraries to find other potential inhibitors. This study explored key molecular interactions between Spiroindolones and PfATP4, opening possibilities for the development of new malaria treatments.