Selection and characterization of peptides binding to diamond-like carbon



: Gabryelczyk B, Szilvay GR, Salomaki M, Laaksonen P, Linder MB

Publisher: ELSEVIER SCIENCE BV

: 2013

: Colloids and Surfaces B: Biointerfaces

: COLLOIDS AND SURFACES B-BIOINTERFACES

: COLLOID SURFACE B

: 110

: 66

: 73

: 8

: 0927-7765

DOI: https://doi.org/10.1016/j.colsurfb.2013.04.002


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.



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