Investigation of Plasmodium falciparum aminopeptidases and characterisation of the M17 leucine aminopeptidase

Abstract

Plasmodium falciparum spends part of its life cycle residing in human erythrocytes, during which time it digests much of the host cell haemoglobin to provide a source of amino acids for synthesis of its own proteins. The final stages of digestion are thought to be carried out by aminopeptidases that cleave amino acids from the N -termini of peptides. The inhibition of aminopeptidase activity can disrupt parasite development, implicating this group of enzymes as a possible drug target. Novel targets for antimalarial drugs are greatly needed due to the high rate of mortality associated with the disease and the emergence of resistance to existing treatments.