Aluminum- and mild steel-binding peptides from phage display |
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Authors: | Rongjun Zuo Dogan Örnek Thomas K. Wood |
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Affiliation: | (1) Departments of Chemical Engineering and Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3222, USA;(2) Present address: Genzyme Corporation, Cambridge, MA 02139, USA |
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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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