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Aluminum- and mild steel-binding peptides from phage display

  • Applied Genetics and Molecular Biotechnology
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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.

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Acknowledgements

This project was supported by the Electric Power Research Institute (contract WO8044-0).

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Author notes

  1. Dogan Örnek

    Present address: Genzyme Corporation, Cambridge, MA 02139, USA

Authors and Affiliations

  1. Departments of Chemical Engineering and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3222, USA

    Rongjun Zuo, Dogan Örnek & Thomas K. Wood

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  1. Rongjun Zuo
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  2. Dogan Örnek
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  3. Thomas K. Wood
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Correspondence to Thomas K. Wood.

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Zuo, R., Örnek, D. & Wood, T.K. Aluminum- and mild steel-binding peptides from phage display. Appl Microbiol Biotechnol 68, 505–509 (2005). https://doi.org/10.1007/s00253-005-1922-5

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  • DOI: https://doi.org/10.1007/s00253-005-1922-5

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