Molecular docking studies of novel 9-aminoacridines with potential antimalarial activity

: The aim


Molecular docking studies of novel 9-aminoacridines with potential antimalarial activity Introduction
Hemoglobin degradation in a parasitic acidic vacuole represents a major metabolic pathway which is essential for the intraerythrocytic development of malaria parasites 1 .
Four members of a family of P. falciparum aspartic proteinases termed as digestive plasmepsins (PMI, PMII, PMIV and HAP) have shown to be able to degrade hemoglobin in vitro 2,3 .
Previous studies have shown that antimalarial activity of acridine derivatives is based on inhibition of hemozoin formation 4 , inhibition of DNA topoisomerase 5 , folate metabolism inhibition 6 and plasmepsin II inhibition 7 .

Results and discussion
Derivatives with binding energies similar to the corresponding co-crystallized ligand KNI-10006 which form some of the key binding interactions with PMI were:    -8.0 5. -8.9 6.

Table 9 .
Binding energies of co-crystallized ligand and derivative 6