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- SVSVGMKPSPRP: a broad range adhesion peptide doi link

Auteur(s): Estephan Elias, Dao Jérome, Saab Marie-Belle, Panayotov Ivan, Martin Fernandez M., Larroque Christian, Gergely C., Cuisinier Frédéric J. G., Levallois Bernard

(Article) Publié: Biomedizinische Technik / Biomedical Engineering, vol. p.10.1515/bmt-2011-0109 (2012)
Texte intégral en Openaccess : istex


Ref HAL: hal-00755416_v1
PMID 23183721
DOI: 10.1515/bmt-2011-0109
WoS: 000312707900008
Exporter : BibTex | endNote
15 Citations
Résumé:

Background: A combinatorial phage display approach was previously used to evolve a 12-mer peptide (SVSVGMKP- SPRP) with the highest affinity for different semiconductor surfaces.Thediscoveryofthemultipleoccurrencesofthe 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 inor- ganic 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.