Abstract
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 K(i) values of less than 0.1n M suggesting successful hydrophobic interactions.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antimalarials / chemistry*
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Antimalarials / pharmacology
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Aspartic Acid Endopeptidases / antagonists & inhibitors*
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Aspartic Acid Endopeptidases / chemistry
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Biomimetic Materials / chemistry*
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Biomimetic Materials / pharmacology
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry*
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Oligopeptides / pharmacology
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Phenylbutyrates / chemistry*
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Plasmodium falciparum / enzymology*
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Protease Inhibitors / chemistry*
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Protease Inhibitors / pharmacology
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Protein Conformation
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Protozoan Proteins
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Structure-Activity Relationship
Substances
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Antimalarials
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KNI 10006
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Oligopeptides
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Phenylbutyrates
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Protease Inhibitors
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Protozoan Proteins
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3-amino-2-hydroxy-4-phenylbutanoic acid
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Aspartic Acid Endopeptidases
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plasmepsin II