Selection and characterization of peptides binding to diamond-like carbon
- VTT Technical Research Centre of Finland
- University of Turku
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 pill 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/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. (c) 2013 Elsevier B.V. All rights reserved.
|Julkaisu||Colloids and Surfaces B: Biointerfaces|
|Tila||Julkaistu - 1 lokakuuta 2013|
|OKM-julkaisutyyppi||A1 Julkaistu artikkeli, soviteltu|