Plasmepsin group of enzymes are key enzymes in the life cycle of malarial 
parasites. As inhibition of plasmepsins leads to the parasite's death, these 
enzymes can be utilized as potential drug targets. Although many drugs are 
available, it has been observed that Plasmodium falciparum, the species that 
causes most of the malarial infections and subsequent death, has developed 
resistance against most of the drugs. Based on the cleavage sites of hemglobin, 
the substrate for plasmepsins, we have designed two compounds 
(p-nitrobenzoyl-leucine-beta-alanine and p-nitrobenzoyl-leucine-isonipecotic 
acid), synthesized them, solved their crystal structures and studied their 
inhibitory effect using experimental and theoretical (docking) methods. In this 
paper, we discuss the synthesis, crystal structures and inhibitory nature of 
these two compounds which have a potential to inhibit plasmepsins.