Synthesis and influenza virus inhibitory activities of carbosilane dendrimers peripherally functionalized with hemagglutinin-binding peptide

Ken Hatano, Teruhiko Matsubara, Yosuke Muramatsu, Masakazu Ezure, Tetsuo Koyama, Koji Matsuoka, Ryunosuke Kuriyama, Haruka Kori, Toshinori Sato

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

A series of carbosilane dendrimers uniformly functionalized with hemagglutinin (HA) binding peptide (sialic acid-mimic peptide, Ala-Arg-Leu-Pro-Arg) was systematically synthesized, and their anti-influenza virus activity was evaluated. The carbosilane-based peptide dendrimers, unlike sialylated dendrimers, cannot be digested by virus neuraminidases. The peptide dendrimers exhibited intriguing biological activities depending on the form of their core frame, with a dumbbell-type peptide dendrimer showing particularly strong inhibitory activities against two human influenza viruses, A/PR/8/34 (H1N1) and A/Aichi/2/68 (H3N2). The IC50 values of the dumbbell-type peptide dendrimer for both strains were 0.60 μM, the highest activity among the HA-binding peptide derivatives. The results suggest that a dumbbell-shaped carbosilane dendrimer is the most suitable core scaffold for HA-binding peptide dendrimers.

Original languageEnglish
Pages (from-to)8332-8339
Number of pages8
JournalJournal of Medicinal Chemistry
Volume57
Issue number20
DOIs
Publication statusPublished - 2014 Oct 23

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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