Selection of novel structural zinc sites from a random peptide library

Teruhiko Matsubara, Yuko Hiura, Osamu Kawahito, Mikito Yasuzawa, Katsuhiro Kawashiro

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


Zinc ion (Zn2+) can be coordinated with four or three amino acid residues to stabilize a protein's structure or to form a catalytic active center. We used phage display selection of a dodecamer random peptide library with Zn2+ to identify structural zinc sites. The binding specificity for Zn2+ of selected sequences was confirmed using enzyme-linked immunosorbent and competitive inhibition assays. Circular dichroism spectra indicated that the interaction with Zn2+ induced a change in conformation, which means the peptide acts as a structural zinc site. Furthermore, a search of protein databases revealed that two selected sequences corresponded to parts of natural zinc sites of copper/zinc superoxide dismutase and zinc-containing ferredoxin. We demonstrated that Zn2+-binding sequences selected from the random combinatorial library would be candidates for artificial structural zinc sites.

Original languageEnglish
Pages (from-to)317-321
Number of pages5
JournalFEBS Letters
Issue number2
Publication statusPublished - 2003 Dec 4


  • Metalloenzyme
  • Phage display system
  • Random peptide library
  • Sequence homology
  • Structural zinc

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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