Plasmepsin II (PM II) is an attractive target for anti-malaria drug discovery, 
which involves in host hemoglobin degradation in the acidic food vacuole. In 
this study, we demonstrated the successful use of structure-based virtual 
screening to identify inhibitors of PM II from two chemical database. Five novel 
non-peptide inhibitors were identified and revealed moderate inhibitory 
potencies with IC50 ranged from 4.62 ± 0.39 to 9.47 ± 0.71 μM. The detailed 
analysis of binding modes using docking simulations for five inhibitors showed 
that the inhibitors could be stabilized by forming multiple hydrogen bonds with 
catalytic residues (Asp 34 and Asp 214) and also with other key residues.