Additional interaction of allophenylnorstatine-containing tripeptidomimetics with malarial aspartic protease plasmepsin II

Based on a highly potent allophenylnorstatine-containing inhibitor, KNI-10006, against the plasmepsins of Plasmodium falciparum, we synthesized a series of tripeptide-type compounds with various N-terminal moieties and evaluated their inhibitory activities against plasmepsin II. Certain phenylacetyl derivatives exhibited extremely high affinity with Ki values of less than 0.1 nM suggesting successful hydrophobic interactions.

A series of allophenylnorstatine-containing tripeptidic compounds were synthesized with various N-terminal phenylacetyl moieties. Certain derivatives exhibited extremely potent inhibitory activity against plasmepsin II.Figure optionsDownload as PowerPoint slide