Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability

Daisuke Kase, John L. Kulp, Masako Yudasaka, John Evans, Sumio Iijima, Kiyotaka Shiba

Research output: Contribution to journalArticle

Abstract

The identification of peptide aptamer with conformational variability was described using affinity selection of peptide phage libraries against single-wall carbon nanohorns (SWHN). The SWHNs were prepared by CO 2 laser ablation under an Ar gas atmosphere at room temperature. After six rounds of M13 phage library, an increase in ratio of bound to input phages was observed, which indicated that SWNH-binding phages were concentrated in mixture. The results show that M13 phage display technology enables to identify a 12-amino-acid pIII tail sequence, DYFSSPYYEQLF, which exhibits a binding preference for SWNH surfaces.

Original languageEnglish (US)
Pages (from-to)8939-8941
Number of pages3
JournalLangmuir
Volume20
Issue number20
DOIs
StatePublished - Sep 28 2004

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Peptide Aptamers
Nanohorns
Bacteriophages
Peptides
peptides
affinity
Carbon
carbon
laser ablation
amino acids
atmospheres
room temperature
gases
Laser ablation
Carbon Monoxide
Amino acids
Gases
Display devices
Amino Acids

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability. / Kase, Daisuke; Kulp, John L.; Yudasaka, Masako; Evans, John; Iijima, Sumio; Shiba, Kiyotaka.

In: Langmuir, Vol. 20, No. 20, 28.09.2004, p. 8939-8941.

Research output: Contribution to journalArticle

Kase, Daisuke ; Kulp, John L. ; Yudasaka, Masako ; Evans, John ; Iijima, Sumio ; Shiba, Kiyotaka. / Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability. In: Langmuir. 2004 ; Vol. 20, No. 20. pp. 8939-8941.
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