Aluminum- and mild steel-binding peptides from phage display

Rongjun Zuo, Dogan Örnek, Thomas Keith Wood

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Using a phage library displaying random peptides of 12 amino acids on its surface, several peptides were found that bind to aluminum and mild steel. Like other metal-binding peptides, no obvious consensus motif has been found for these peptides. However, most of them are rich in hydroxyl-containing amino acids, serine or threonine, or contain histidine. For the aluminum-binding peptides, peptides with a higher number of hydroxyl-containing amino acids bind to the aluminum surface more tightly. For example, Val-Pro-Ser-Ser-Gly-Pro-Gln- Asp-Thr-Arg-Thr-Thr, which contains five hydroxyl-containing amino acid residues, was selected four-fold more frequently than a peptide containing only one serine, suggesting an important role for the hydroxyl-containing amino acids in the metal-peptide interaction.

Original languageEnglish (US)
Pages (from-to)505-509
Number of pages5
JournalApplied Microbiology and Biotechnology
Volume68
Issue number4
DOIs
StatePublished - Sep 1 2005

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Bacteriophages
Steel
Aluminum
Peptides
Carbon steel
Display devices
Amino acids
Hydroxyl Radical
Amino Acids
Serine
Metals
Peptide Library
Threonine
Histidine

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Microbiology
  • Bioengineering
  • Microbiology (medical)

Cite this

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Aluminum- and mild steel-binding peptides from phage display. / Zuo, Rongjun; Örnek, Dogan; Wood, Thomas Keith.

In: Applied Microbiology and Biotechnology, Vol. 68, No. 4, 01.09.2005, p. 505-509.

Research output: Contribution to journalArticle

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