Selection and characterization of peptides binding to diamond-like carbon

Bartosz Gabryelczyk, Géza Szilvay, Mikko Salomäki, Päivi Laaksonen, Markus Linder (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    6 Citations (Scopus)


    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 63 nM and the maximum binding capacity was 6.8 pmol/cm2. 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.
    Original languageEnglish
    Pages (from-to)66-73
    JournalColloids and Surfaces B: Biointerfaces
    Publication statusPublished - 2013
    MoE publication typeA1 Journal article-refereed


    • alkaline phosphatase
    • diamond-like carbon
    • ellipsometry
    • inorganic binding peptides
    • phage display
    • protein adsorption


    Dive into the research topics of 'Selection and characterization of peptides binding to diamond-like carbon'. Together they form a unique fingerprint.

    Cite this