Disruption of the AMA1–RON2 interaction in the invasion of red blood cells by malarial parasites represents a promising avenue for antimalarial drug discovery.
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10">A 13-residue β-hairpin based on the C-terminal loop of RON2 was used to probe a conserved binding site on AMA1 and facilitated the identification of two beneficial interactions.
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15">Crystal structures of several β-hairpin peptides in complex with AMA1 have been determined to define the structural features that contribute to improved binding affinity.
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Introduction of two beneficial mutations into the longer RON2sp2 peptide produced the most potent strain-transcending peptide inhibitor reported for AMA1 to date.
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