Molecular evolution of GM3-binding peptides using a phage display method

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Influenza virus 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 ganglioside GM3 (Neu5Acα2-3Galβ1-4Glcβ1-1'ceramide)-binding pentadecapeptide has been obtained from a random phage-displayed peptide library. However, since the phage library employed in our previous study did not have enough diversity, we attempted the directed evolution to improve the binding affinity of the GM3-binding peptide (c01). We constructed the randomized sublibrary of c01 with its diversity of about two million recombinants. Four round of the affinity selection against GM3 monolayer was performed and the binding affinities of the isolated phage clones to glycolipids were analyzed by ELISA. Two phage clones (4-11 and 4-16) showed high affinity for GM3 rather than that of the original c01 peptide, moreover the binding specificity of the 4-11 clone improved.

Original languageEnglish
Title of host publicationPolymer Preprints, Japan
Pages2082
Number of pages1
Volume54
Edition1
Publication statusPublished - 2005
Event54th SPSJ Annual Meeting 2005 - Yokohama, Japan
Duration: 2005 May 252005 May 27

Other

Other54th SPSJ Annual Meeting 2005
CountryJapan
CityYokohama
Period05/5/2505/5/27

Fingerprint

Bacteriophages
Peptides
Display devices
Viruses
Ceramides
Sugars
Monolayers

Keywords

  • GM3
  • Influenza virus
  • Molecular evolution
  • Peptide
  • Phage library

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Kubota, H., Matsubara, T., & Sato, T. (2005). Molecular evolution of GM3-binding peptides using a phage display method. In Polymer Preprints, Japan (1 ed., Vol. 54, pp. 2082)

Molecular evolution of GM3-binding peptides using a phage display method. / Kubota, Hiroyuki; Matsubara, Teruhiko; Sato, Toshinori.

Polymer Preprints, Japan. Vol. 54 1. ed. 2005. p. 2082.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Kubota, H, Matsubara, T & Sato, T 2005, Molecular evolution of GM3-binding peptides using a phage display method. in Polymer Preprints, Japan. 1 edn, vol. 54, pp. 2082, 54th SPSJ Annual Meeting 2005, Yokohama, Japan, 05/5/25.
Kubota H, Matsubara T, Sato T. Molecular evolution of GM3-binding peptides using a phage display method. In Polymer Preprints, Japan. 1 ed. Vol. 54. 2005. p. 2082
Kubota, Hiroyuki ; Matsubara, Teruhiko ; Sato, Toshinori. / Molecular evolution of GM3-binding peptides using a phage display method. Polymer Preprints, Japan. Vol. 54 1. ed. 2005. pp. 2082
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