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 Spencer Evans, Sumio Iijima, Kiyotaka Shiba

Research output: Contribution to journalArticlepeer-review

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

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

Fingerprint Dive into the research topics of 'Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability'. Together they form a unique fingerprint.

Cite this