Selection and characterization of peptides binding to diamond-like carbon

Research output: Contribution to journalArticleScientificpeer-review

Researchers

Research units

  • VTT Technical Research Centre of Finland
  • University of Turku

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 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.

Details

Original languageEnglish
Pages (from-to)66-73
Number of pages8
JournalColloids and Surfaces B: Biointerfaces
Volume110
Publication statusPublished - 1 Oct 2013
MoE publication typeA1 Journal article-refereed

    Research areas

  • Diamond-like carbon, Inorganic binding peptides, Alkaline phosphatase, Phage display, Ellipsometry, Protein adsorption, PHAGE DISPLAY, ESCHERICHIA-COLI, HIGH-AFFINITY, REPEATING POLYPEPTIDES, BIOMIMETIC COMPOSITES, ALKALINE-PHOSPHATASE, PROTEIN ADSORPTION, DLC COATINGS, SURFACE, BEHAVIOR

ID: 891710