Selection and characterization of peptides binding to diamond-like carbon

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Selection and characterization of peptides binding to diamond-like carbon. / Gabryelczyk, Bartosz; Szilvay, Geza R.; Salomäki, Mikko; Laaksonen, Päivi; Linder, Markus B.

In: Colloids and Surfaces B: Biointerfaces, Vol. 110, 01.10.2013, p. 66-73.

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@article{e09c6da3132f451db26825d40115623d,
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 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.",
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",
author = "Bartosz Gabryelczyk and Szilvay, {Geza R.} and Mikko Salom{\"a}ki and P{\"a}ivi Laaksonen and Linder, {Markus B.}",
year = "2013",
month = "10",
day = "1",
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 Science B.V.",

}

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TY - JOUR

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

AU - Gabryelczyk, Bartosz

AU - Szilvay, Geza R.

AU - Salomäki, Mikko

AU - Laaksonen, Päivi

AU - Linder, Markus B.

PY - 2013/10/1

Y1 - 2013/10/1

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 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.

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 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.

KW - Diamond-like carbon

KW - Inorganic binding peptides

KW - Alkaline phosphatase

KW - Phage display

KW - Ellipsometry

KW - Protein adsorption

KW - PHAGE DISPLAY

KW - ESCHERICHIA-COLI

KW - HIGH-AFFINITY

KW - REPEATING POLYPEPTIDES

KW - BIOMIMETIC COMPOSITES

KW - ALKALINE-PHOSPHATASE

KW - PROTEIN ADSORPTION

KW - DLC COATINGS

KW - SURFACE

KW - BEHAVIOR

U2 - 10.1016/j.colsurfb.2013.04.002

DO - 10.1016/j.colsurfb.2013.04.002

M3 - Article

VL - 110

SP - 66

EP - 73

JO - Colloids and surfaces, B: Biointerfaces

JF - Colloids and surfaces, B: Biointerfaces

SN - 0927-7765

ER -

ID: 891710