title: Selection and characterization of peptides binding to diamond-like carbon.
abstract: Phage display was used to find peptides specific for amorphous diamond-like carbon (DLC). A set of putative binders was analyzed in detail and one sequence was found that functioned both as a peptide fused to the pIII protein in M13 phage and as a peptide fused to the enzyme alkaline phosphatase (AP). The dissociation constant of the peptide-AP fusion on DLC was 63nM and the maximum binding capacity was 6.8pmol/cm(2). Multiple ways of analysis, including phage titer, enzyme-linked immunosorbent assay, and ellipsometry were used to analyze binding and to exclude possible false positive results. DLC binding peptides can be useful for self-assembling coatings for modifying DLC in specific ways.
authors.affiliation: VTT Technical Research Centre of Finland, P.O. Box 1000, FI-02044 VTT, Espoo, Finland. bartosz.gabryelczyk@vtt.fi
authors.forename: Bartosz
authors.initials: B
authors.lastname: Gabryelczyk
authors.forename: Géza R
authors.initials: GR
authors.lastname: Szilvay
authors.forename: Mikko
authors.initials: M
authors.lastname: Salomäki
authors.forename: Päivi
authors.initials: P
authors.lastname: Laaksonen
authors.forename: Markus B
authors.initials: MB
authors.lastname: Linder
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002244:Carbon / Q000737:chemistry*; D010316:Particle Size; D010455:Peptides / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D010455:Peptides; D002244:Carbon; D000469:Alkaline Phosphatase