Selection and characterization of peptides binding to diamond-like carbon

Bartosz Gabryelczyk, Geza R. Szilvay, Mikko Salomäki, Päivi Laaksonen, Markus B. Linder*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

5 Citations (Scopus)

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.

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

Keywords

  • 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

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