Malaria is a devastating human parasitic disease that receives enhanced attention due to the emergence of resistance
to traditional drugs. Thus, the search for new molecular targets is a major goal. PfAM1 is an aminopeptidase from
Plasmodium falciparum, William H. Welch 1897, belonging to the M1 family of metalloproteases, which is a promising target
of inhibitors to block the intra-erythrocytic stages of the parasite. Since its identification in 1998, many efforts have been
done to validate PfAM1 as an appropriate target of antimalarials. The present work is a critical review of the main structural,
functional and kinetic characteristics of PfAM1, as well as a summary of the effects of key inhibitors at molecular and cellular
levels. The systematization of experimental results should contribute to a better understanding of the properties of PfAM1
as a target of antimalarials and promote research projects focused on the development of PfAM1 inhibitors.
Keywords: Antimalarials, growth inhibition, M1 family, metallo-aminopeptidases, Plasmodium falciparum, protease inhibitors.
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