Inhibition of influenza virus infection by minimized peptides which bind to hemagglutinin

Research output: Contribution to conferencePaperpeer-review


Influenza virus hemagglutinin (HA) binds to sialylgalactose (Neu5Ac-Gal) structure on host cells at the first step of infection. The peptide drugs are able to block the virus-sugar interaction. In our previous study, the HA-binding pentadecapeptide has been obtained from a random phage-displayed peptide library. However, it is considered that all amino acid residues are not involved in the interaction with HA, because the size of sugarbinding pocket in HA is too small to fill with pentadecapeptide. In order to identify the active residues, several peptide fragments were prepared. Plaque assay indicated that a N-terminal fragment had a high inhibition activity for influenza virus infection than the corresponding original peptide. We finally identified minimized HA-binding peptide. Furthermore, we showed that stearyl peptide was suitable for aggregate formation that was essential for inhibition of influenza virus infection.

Original languageEnglish
Number of pages1
Publication statusPublished - 2006 Oct 19
Event55th SPSJ Annual Meeting - Nagoya, Japan
Duration: 2006 May 242006 May 26


Other55th SPSJ Annual Meeting


  • Hemagglutinin
  • Influenza virus
  • Peptide
  • Phage display method

ASJC Scopus subject areas

  • General Engineering


Dive into the research topics of 'Inhibition of influenza virus infection by minimized peptides which bind to hemagglutinin'. Together they form a unique fingerprint.

Cite this