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 language | English (US) |
|---|---|
| Pages (from-to) | 505-509 |
| Number of pages | 5 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 68 |
| Issue number | 4 |
| DOIs | |
| State | Published - Sep 2005 |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Applied Microbiology and Biotechnology
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