Multivalent Effect in Influenza Hemagglutinin-Binding Activity of Sugar-Mimic Peptide

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  • MATSUBARA Teruhiko
    Department of Biosciences and Informatics, Faculty of Science and Engineering, Keio University
  • ONISHI Ai
    Department of Biosciences and Informatics, Faculty of Science and Engineering, Keio University
  • SAITO Tomomi
    Department of Biosciences and Informatics, Faculty of Science and Engineering, Keio University
  • YAMAGUCHI Daisuke
    Department of Biosciences and Informatics, Faculty of Science and Engineering, Keio University
  • SATO Toshinori
    Department of Biosciences and Informatics, Faculty of Science and Engineering, Keio University

Bibliographic Information

Other Title
  • 糖鎖模倣ペプチドのインフルエンザヘマグルチニンに対する結合活性の多価効果
  • トウサ モホウ ペプチド ノ インフルエンザヘマグルチニン ニ タイスル ケツゴウ カッセイ ノ タカ コウカ

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Description

Hemagglutinin (HA) of the influenza virus binds to sialyloligosaccaride receptors on the cell surface in the first step of infection; therefore, inhibitors of the HA-receptor interaction have potential as anti-influenza drugs. We previously identified the HA-binding peptide s2, ARLPRTMVHPKPAQP, from random peptide libraries using phage-display technology. The N-stearoyl s2 peptide showed inhibitory activity against influenza virus infection. To obtain molecules with high affinity for HAs, truncated s2 peptides and dendrimers were designed in the present study. The affinity of dendrimers functionalized with the truncated peptide was higher than that of the full-length s2 peptide, especially a tetrameric dendrimer with ARLPR was more than 70-times more effective than the s2 peptide.

Journal

  • KOBUNSHI RONBUNSHU

    KOBUNSHI RONBUNSHU 73 (1), 62-68, 2016

    The Society of Polymer Science, Japan

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