title: Aluminum- and mild steel-binding peptides from phage display.
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.
authors.affiliation: Department of Chemical Engineering, University of Connecticut, Storrs, CT 06269-3222, USA.
authors.forename: Rongjun
authors.initials: R
authors.lastname: Zuo
authors.forename: Dogan
authors.initials: D
authors.lastname: Ornek
authors.forename: Thomas K
authors.initials: TK
authors.lastname: Wood
mesh_terms: D000535:Aluminum / Q000737:chemistry*; D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry*; D019151:Peptide Library; D013232:Steel / Q000737:chemistry*
chemical_list: D010446:Peptide Fragments; D019151:Peptide Library; D013232:Steel; D000535:Aluminum