Biocombinatorial selection of metal ion-chelating peptides

Teruhiko Matsubara; Yuko Hiura; Katsuhiro Kawashiro

doi:10.1142/s0217979203018946

Biocombinatorial selection of metal ion-chelating peptides

Teruhiko Matsubara, Yuko Hiura, Katsuhiro Kawashiro

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

A phage-displayed library selection was performed to obtain metal ion-chelating peptides. A dodecamer (12-mer) random peptide library was displayed on the surface of filamentous bacterial phage and subjected to an affinity selection. Four rounds of the selection gave fourteen Zn²⁺-positive phage clones. Enzyme-linked immunosorbent assay showed that the selected clones specifically bound to Zn²⁺ and Ni²⁺, but not to Cu²⁺ and Fe³⁺. Deduced amino acid sequences of the clones had histidinerich consensus motifs. These chelating peptides should be applied to designing for metal ion-trapping biomaterials.

Original language	English
Pages (from-to)	1324-1328
Number of pages	5
Journal	International Journal of Modern Physics B
Volume	17
Issue number	8-9 I
DOIs	https://doi.org/10.1142/s0217979203018946
Publication status	Published - 2003 Apr 10
Externally published	Yes

ASJC Scopus subject areas

Statistical and Nonlinear Physics
Condensed Matter Physics

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abstract = "A phage-displayed library selection was performed to obtain metal ion-chelating peptides. A dodecamer (12-mer) random peptide library was displayed on the surface of filamentous bacterial phage and subjected to an affinity selection. Four rounds of the selection gave fourteen Zn2+-positive phage clones. Enzyme-linked immunosorbent assay showed that the selected clones specifically bound to Zn2+ and Ni2+, but not to Cu2+ and Fe3+. Deduced amino acid sequences of the clones had histidinerich consensus motifs. These chelating peptides should be applied to designing for metal ion-trapping biomaterials.",

author = "Teruhiko Matsubara and Yuko Hiura and Katsuhiro Kawashiro",

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AU - Hiura, Yuko

AU - Kawashiro, Katsuhiro

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AB - A phage-displayed library selection was performed to obtain metal ion-chelating peptides. A dodecamer (12-mer) random peptide library was displayed on the surface of filamentous bacterial phage and subjected to an affinity selection. Four rounds of the selection gave fourteen Zn2+-positive phage clones. Enzyme-linked immunosorbent assay showed that the selected clones specifically bound to Zn2+ and Ni2+, but not to Cu2+ and Fe3+. Deduced amino acid sequences of the clones had histidinerich consensus motifs. These chelating peptides should be applied to designing for metal ion-trapping biomaterials.

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Biocombinatorial selection of metal ion-chelating peptides

Abstract

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