Selection and characterization of peptides binding to diamond-like carbon

Bartosz Gabryelczyk; Géza Szilvay; Mikko Salomäki; Päivi Laaksonen; Markus Linder

doi:10.1016/j.colsurfb.2013.04.002

Selection and characterization of peptides binding to diamond-like carbon

Bartosz Gabryelczyk, Géza Szilvay, Mikko Salomäki, Päivi Laaksonen, Markus Linder (Corresponding Author)

Research output: Contribution to journal › Article › Scientific › peer-review

6 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 language	English
Pages (from-to)	66-73
Journal	Colloids and Surfaces B: Biointerfaces
Volume	110
DOIs	https://doi.org/10.1016/j.colsurfb.2013.04.002
Publication status	Published - 2013
MoE publication type	A1 Journal article-refereed

Keywords

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

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10.1016/j.colsurfb.2013.04.002

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title = "Selection and characterization of peptides binding to diamond-like carbon",

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.",

keywords = "alkaline phosphatase, diamond-like carbon, ellipsometry, inorganic binding peptides, phage display, protein adsorption",

author = "Bartosz Gabryelczyk and G{\'e}za Szilvay and Mikko Salom{\"a}ki and P{\"a}ivi Laaksonen and Markus Linder",

year = "2013",

doi = "10.1016/j.colsurfb.2013.04.002",

language = "English",

volume = "110",

pages = "66--73",

journal = "Colloids and Surfaces B: Biointerfaces",

issn = "0927-7765",

publisher = "Elsevier",

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TY - JOUR

T1 - Selection and characterization of peptides binding to diamond-like carbon

AU - Gabryelczyk, Bartosz

AU - Szilvay, Géza

AU - Salomäki, Mikko

AU - Laaksonen, Päivi

AU - Linder, Markus

PY - 2013

Y1 - 2013

N2 - 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.

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.

KW - alkaline phosphatase

KW - diamond-like carbon

KW - ellipsometry

KW - inorganic binding peptides

KW - phage display

KW - protein adsorption

U2 - 10.1016/j.colsurfb.2013.04.002

DO - 10.1016/j.colsurfb.2013.04.002

M3 - Article

SN - 0927-7765

VL - 110

SP - 66

EP - 73

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

ER -

Selection and characterization of peptides binding to diamond-like carbon

Abstract

Keywords

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