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SVSVGMKPSPRP: a broad range adhesion peptide.

作者信息

Estephan Elias, Dao Jérôme, Saab Marie-Belle, Panayotov Ivan, Martin Marta, Larroque Christian, Gergely Csilla, Cuisinier Frédéric J G, Levallois Bernard

机构信息

Université Montpellier 2, Laboratoire Charles Coulomb UMR 5221, F-34095, Montpellier, France.

出版信息

Biomed Tech (Berl). 2012 Dec;57(6):481-9. doi: 10.1515/bmt-2011-0109.

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.

摘要

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