Selection and characterization of peptides binding to diamond-like carbon

Bartosz Gabryelczyk, Geza Szilvay, M. Salomäki, Päivi Laaksonen, Markus Linder (Corresponding Author)

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 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
Number of pages7
JournalColloids and Surfaces B: Biointerfaces
Volume110
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Keywords

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

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

Cite this