Selection of novel structural zinc sites from a random peptide library

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

研究成果: Article査読

23 被引用数 (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.

ジャーナルFEBS Letters
出版ステータスPublished - 2003 12月 4

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学


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