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

Koushi Hidaka, Tooru Kimura, Yumi Tsuchiya, Mami Kamiya, Adam J. Ruben, Ernesto Freire, Yoshio Hayashi, Yoshiaki Kiso

Research output: Contribution to journalArticlepeer-review

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 Ki values of less than 0.1 nM suggesting successful hydrophobic interactions.

Original languageEnglish (US)
Pages (from-to)3048-3052
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Volume17
Issue number11
DOIs
StatePublished - Jun 1 2007

Keywords

  • Allophenylnorstatine
  • Aspartic protease
  • Malaria
  • Peptidomimetic
  • Plasmepsin inhibitor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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