Understanding the structure and function of Plasmodium aminopeptidases to facilitate drug discovery

• Published in: Current opinion in structural biology Vol. 82; p. 102693
• Main Authors: Mansouri, Mahta, Daware, Kajal, Webb, Chaille T., McGowan, Sheena
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01-10-2023
• ISSN: 0959-440X; 1879-033X; 1879-033X
• DOI: 10.1016/j.sbi.2023.102693

Malaria continues to be the most widespread parasitic disease affecting humans globally. As parasites develop drug resistance at an alarming pace, it has become crucial to identify novel drug targets. Over the last decade, the metalloaminopeptidases have gained importance as potential targets for new antimalarials. These enzymes are responsible for removing the N-terminal amino acids from proteins and peptides, and their restricted specificities suggest that many perform unique and essential roles within the malaria parasite. This mini-review focuses on the recent progress in structure and functional data relating to the Plasmodium metalloaminopeptidases that have been validated or shown promise as new antimalarial drug targets.