Biocombinatorial selection of metal ion-chelating peptides

Teruhiko Matsubara, Yuko Hiura, Katsuhiro Kawashiro

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)1324-1328
Number of pages5
JournalInternational Journal of Modern Physics B
Volume17
Issue number8-9 I
Publication statusPublished - 2003 Apr 10
Externally publishedYes

Fingerprint

Bacteriophages
Chelation
Clone
Peptides
peptides
Metal ions
metal ions
Metals
Biomaterials
Enzyme-linked Immunosorbent Assay
Peptide Library
Immunosorbents
Biocompatible Materials
Amino Acid Sequence
Trapping
Affine transformation
amino acids
affinity
Amino acids
enzymes

ASJC Scopus subject areas

  • Physics and Astronomy (miscellaneous)
  • Condensed Matter Physics
  • Electronic, Optical and Magnetic Materials
  • Statistical and Nonlinear Physics
  • Mathematical Physics

Cite this

Biocombinatorial selection of metal ion-chelating peptides. / Matsubara, Teruhiko; Hiura, Yuko; Kawashiro, Katsuhiro.

In: International Journal of Modern Physics B, Vol. 17, No. 8-9 I, 10.04.2003, p. 1324-1328.

Research output: Contribution to journalArticle

Matsubara, Teruhiko ; Hiura, Yuko ; Kawashiro, Katsuhiro. / Biocombinatorial selection of metal ion-chelating peptides. In: International Journal of Modern Physics B. 2003 ; Vol. 17, No. 8-9 I. pp. 1324-1328.
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