Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials

Tina S. Skinner-Adams, Colin M. Stack, Katharine R. Trenholme, Chris L. Brown, Jolanta Grembecka, Jonathan Lowther, Artur Mucha, Marcin Drag, Pawel Kafarski, Sheena McGowan, James C. Whisstock, Donald L. Gardiner, John P. Dalton

Research output: Contribution to journalLiterature reviewpeer-review


The neutral aminopeptidases M1 alanyl aminopeptidase (PfM1AAP) and M17 leucine aminopeptidase (PfM17LAP) of the human malaria parasite Plasmodium falciparum are targets for the development of novel anti-malarial drugs. Although the functions of these enzymes remain unknown, they are believed to act in the terminal stages of haemoglobin degradation, generating amino acids essential for parasite growth and development. Inhibitors of both enzymes are lethal to P. falciparum in culture and kill the murine malaria P. chabaudi in vivo. Recent biochemical, structural and functional studies provide the substrate specificity and mechanistic binding data needed to guide the development of more potent antimalarial drugs. Together with biological studies, these data form the rationale for choosing PfM1AAP and PfM17LAP as targets for anti-malarial development.

Original languageEnglish
Pages (from-to)53-61
Number of pages9
JournalTrends in biochemical sciences
Issue number1
Publication statusPublished - Jan 2010


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