PTEX is the Plasmodium translocon of exported proteins of the malaria parasite (Plasmodium sp.) and functions to export proteins out of the parasite vacuolar membrane, remodeling the host erythrocyte. Remodeling enables the parasite to access vital nutrients and avoid immune defense of the host, enabling parasite survival and leading to malaria disease. A key protein interaction in PTEX involves 12 residues of component EXP2, which form an augmented β-sheet with component HSP101. Theoretically, interrupting this essential interaction by introducing a peptide corresponding to these 12 residues of EXP2 to compete with endogenous EXP2 would fatally damage the protein transport mechanism. If utilized therapeutically, this peptide could inhibit function of PTEX, thereby protecting host erythrocyte from parasitic use of nutrients and proteins, ultimately leading to parasite death.