The World Health Organization (WHO) estimated about 207 million malaria cases and 627,000 malaria deaths around the world in 2012. The malarial parasite Plasmodium falciparum digests hemoglobin as a source of essential nutrients by using its proteases such as plasmepsin II to break down the hemoglobin. However, Sickle hemoglobin, which has a one-residue mutation compared to normal hemoglobin has shown some natural resistance to infection from P. falciparum. In this study, the docking of plasmepsin II to the dimer conformation of normal and sickle human hemoglobin were investigated to identify potential differences. The docking study identified potential binding modes of plasmepsin II to both normal and sickle hemoglobin involving binding either to the α or β chain, or docked between the chains. In both cases the α chain was highly favorable to plasmepsin docking. A few residues in plasmepsin II have been identified to be highly active in all binding modes. Further exploration into the binding energies, effect of mutations and electrostatic calculation will be conducted.

Docking studies of binding of Plasmodium falciparum plasmepsin II to normal and sickle hemoglobin

249th National Meeting (2015)

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