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

Fingerprint

Diamond
Peptides
Bacteriophages
peptides
Diamonds
Carbon
diamonds
carbon
enzymes
Enzymes
Bacteriophage M13
Immunosorbents
phosphatases
Phosphatases
Ellipsometry
assembling
ellipsometry
Binders
Alkaline Phosphatase
Assays

Keywords

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

Cite this

Gabryelczyk, Bartosz ; Szilvay, Geza ; Salomäki, M. ; Laaksonen, Päivi ; Linder, Markus. / Selection and characterization of peptides binding to diamond-like carbon. In: Colloids and Surfaces B: Biointerfaces. 2013 ; Vol. 110. pp. 66-73.
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Selection and characterization of peptides binding to diamond-like carbon. / Gabryelczyk, Bartosz; Szilvay, Geza; Salomäki, M.; Laaksonen, Päivi; Linder, Markus (Corresponding Author).

In: Colloids and Surfaces B: Biointerfaces, Vol. 110, 2013, p. 66-73.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Linder, Markus

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AB - 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.

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