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Biomed Tech (Berl) ; 57(6): 481-9, 2012 Dec.
Article in English | MEDLINE | ID: mdl-23183721

ABSTRACT

BACKGROUND: A combinatorial phage display approach was previously used to evolve a 12-mer peptide (SVSVGMKPSPRP) with the highest affinity for different semiconductor surfaces. The discovery of the multiple occurrences of the SVSVGMKPSPRP sequence in an all-against-all basic local alignment search tool search of PepBank sequences was unexpected, and a Google search using the peptide sequence recovered 58 results concerning 12 patents and 16 scientific publications. The number of patent and articles indicates that the peptide is perhaps a broad range adhesion peptide. METHODS: To evaluate peptide properties, we conducted a study to investigate peptide adhesion on different inorganic substrates by mass spectrometry and atomic force microscopy for gold, carbon nanotubes, cobalt, chrome alloy, titanium, and titanium alloy substrates. RESULTS: Our results showed that the peptide has a great potential as a linker to functionalize metallic surfaces if specificity is not a key factor. This peptide is not specific to a particular metal surface, but it is a good linker for the functionalization of a wide range of metallic materials. CONCLUSION: The fact that this peptide has the potential to adsorb on a large set of inorganic surfaces suggests novel promising directions for further investigation. Affinity determination of SVSVGMKPSPRP peptide would be an important issue for eventual commercial uses.


Subject(s)
Biocompatible Materials/chemistry , Cell Adhesion Molecules/chemistry , Metals/chemistry , Peptides/chemistry , Materials Testing , Protein Binding
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