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

doi:10.1021/la048968m

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 journal › Article › peer-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 language	English (US)
Pages (from-to)	8939-8941
Number of pages	3
Journal	Langmuir
Volume	20
Issue number	20
DOIs	https://doi.org/10.1021/la048968m
State	Published - Sep 28 2004

ASJC Scopus subject areas

General Materials Science
Condensed Matter Physics
Surfaces and Interfaces
Spectroscopy
Electrochemistry

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10.1021/la048968m

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

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.",

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AU - Kase, Daisuke

AU - Kulp, John L.

AU - Yudasaka, Masako

AU - Evans, John Spencer

AU - Iijima, Sumio

AU - Shiba, Kiyotaka

PY - 2004/9/28

Y1 - 2004/9/28

N2 - 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.

AB - 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.

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

Abstract

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