Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry

Marie-Luise Niklew; Ulrike Hochkirch; Anna Melikyan; Thomas Moritz; Sandra Kurzawski; Hartmut Schlüter; Ingo Ebner; Michael W Linscheid

doi:10.1021/ac902403m

Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry

Standard

Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry. / Niklew, Marie-Luise; Hochkirch, Ulrike; Melikyan, Anna; Moritz, Thomas; Kurzawski, Sandra; Schlüter, Hartmut; Ebner, Ingo; Linscheid, Michael W.

In: ANAL CHEM, Vol. 82, No. 3, 3, 01.02.2010, p. 1047-1053.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Niklew, M-L, Hochkirch, U, Melikyan, A, Moritz, T, Kurzawski, S, Schlüter, H, Ebner, I & Linscheid, MW 2010, 'Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry', ANAL CHEM, vol. 82, no. 3, 3, pp. 1047-1053. https://doi.org/10.1021/ac902403m

APA

Niklew, M-L., Hochkirch, U., Melikyan, A., Moritz, T., Kurzawski, S., Schlüter, H., Ebner, I., & Linscheid, M. W. (2010). Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry. ANAL CHEM, 82(3), 1047-1053. [3]. https://doi.org/10.1021/ac902403m

Vancouver

Niklew M-L, Hochkirch U, Melikyan A, Moritz T, Kurzawski S, Schlüter H et al. Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry. ANAL CHEM. 2010 Feb 1;82(3):1047-1053. 3. https://doi.org/10.1021/ac902403m

Bibtex

@article{9989b4f94ddf4a879d91a5c84e8b7e18,

title = "Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry",

abstract = "The use of nanocrystalline titanium dioxide films as affinity targets for the selective isolation and enrichment of phosphopeptides with subsequent analysis by matrix-assisted laser desorption ionization (MALDI) mass spectrometry is described. A strong affinity of phosphopeptides to anatase titanium dioxide surfaces is observed, and a standard protocol for the selective isolation and enrichment of phosphopeptides on titanium dioxide films using a proteolytic digest of alpha- and beta-casein was developed. All washing and elution procedures using these films can be processed directly on the MALDI target, thereby avoiding sample contamination and losses. In addition, the enrichment of the phosphopeptides was improved due to a considerable enlargement of the surface. Several film substrates compatible with routine inlet systems of mass spectrometers, as conductive glass, aluminum, and silicon, have been manufactured and tested. A biological application was examined by the human fibrinogen-thrombin system. For a quantification and comparison of different expression levels of phosphoproteins in biological systems, the peptides were labeled with S-methyl thioimidate reagents. The capability of this method for high-throughput applications make the use of mesoporous titanium dioxide films as an affinity MALDI target a promising tool in phosphoproteomics. A combination of an amidation protocol showed that a quantification of phosphorylated peptides can easily be performed using TiO(2) films.",

keywords = "Animals, Humans, Cattle, Amino Acid Sequence, Molecular Sequence Data, Nanoparticles/*chemistry, Trypsin/metabolism, Caseins/chemistry/metabolism, Fibrinogen/chemistry/metabolism, Phosphopeptides/*analysis, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/*methods, Thrombin/metabolism, Titanium/*chemistry, Animals, Humans, Cattle, Amino Acid Sequence, Molecular Sequence Data, Nanoparticles/*chemistry, Trypsin/metabolism, Caseins/chemistry/metabolism, Fibrinogen/chemistry/metabolism, Phosphopeptides/*analysis, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/*methods, Thrombin/metabolism, Titanium/*chemistry",

author = "Marie-Luise Niklew and Ulrike Hochkirch and Anna Melikyan and Thomas Moritz and Sandra Kurzawski and Hartmut Schl{\"u}ter and Ingo Ebner and Linscheid, {Michael W}",

year = "2010",

month = feb,

day = "1",

doi = "10.1021/ac902403m",

language = "English",

volume = "82",

pages = "1047--1053",

journal = "ANAL CHEM",

issn = "0003-2700",

publisher = "American Chemical Society",

number = "3",

}

RIS

TY - JOUR

T1 - Phosphopeptide screening using nanocrystalline titanium dioxide films as affinity matrix-assisted laser desorption ionization targets in mass spectrometry

AU - Niklew, Marie-Luise

AU - Hochkirch, Ulrike

AU - Melikyan, Anna

AU - Moritz, Thomas

AU - Kurzawski, Sandra

AU - Schlüter, Hartmut

AU - Ebner, Ingo

AU - Linscheid, Michael W

PY - 2010/2/1

Y1 - 2010/2/1

N2 - The use of nanocrystalline titanium dioxide films as affinity targets for the selective isolation and enrichment of phosphopeptides with subsequent analysis by matrix-assisted laser desorption ionization (MALDI) mass spectrometry is described. A strong affinity of phosphopeptides to anatase titanium dioxide surfaces is observed, and a standard protocol for the selective isolation and enrichment of phosphopeptides on titanium dioxide films using a proteolytic digest of alpha- and beta-casein was developed. All washing and elution procedures using these films can be processed directly on the MALDI target, thereby avoiding sample contamination and losses. In addition, the enrichment of the phosphopeptides was improved due to a considerable enlargement of the surface. Several film substrates compatible with routine inlet systems of mass spectrometers, as conductive glass, aluminum, and silicon, have been manufactured and tested. A biological application was examined by the human fibrinogen-thrombin system. For a quantification and comparison of different expression levels of phosphoproteins in biological systems, the peptides were labeled with S-methyl thioimidate reagents. The capability of this method for high-throughput applications make the use of mesoporous titanium dioxide films as an affinity MALDI target a promising tool in phosphoproteomics. A combination of an amidation protocol showed that a quantification of phosphorylated peptides can easily be performed using TiO(2) films.

AB - The use of nanocrystalline titanium dioxide films as affinity targets for the selective isolation and enrichment of phosphopeptides with subsequent analysis by matrix-assisted laser desorption ionization (MALDI) mass spectrometry is described. A strong affinity of phosphopeptides to anatase titanium dioxide surfaces is observed, and a standard protocol for the selective isolation and enrichment of phosphopeptides on titanium dioxide films using a proteolytic digest of alpha- and beta-casein was developed. All washing and elution procedures using these films can be processed directly on the MALDI target, thereby avoiding sample contamination and losses. In addition, the enrichment of the phosphopeptides was improved due to a considerable enlargement of the surface. Several film substrates compatible with routine inlet systems of mass spectrometers, as conductive glass, aluminum, and silicon, have been manufactured and tested. A biological application was examined by the human fibrinogen-thrombin system. For a quantification and comparison of different expression levels of phosphoproteins in biological systems, the peptides were labeled with S-methyl thioimidate reagents. The capability of this method for high-throughput applications make the use of mesoporous titanium dioxide films as an affinity MALDI target a promising tool in phosphoproteomics. A combination of an amidation protocol showed that a quantification of phosphorylated peptides can easily be performed using TiO(2) films.

KW - Animals

KW - Humans

KW - Cattle

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Nanoparticles/chemistry

KW - Trypsin/metabolism

KW - Caseins/chemistry/metabolism

KW - Fibrinogen/chemistry/metabolism

KW - Phosphopeptides/analysis

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods

KW - Thrombin/metabolism

KW - Titanium/chemistry

KW - Animals

KW - Humans

KW - Cattle

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Nanoparticles/chemistry

KW - Trypsin/metabolism

KW - Caseins/chemistry/metabolism

KW - Fibrinogen/chemistry/metabolism

KW - Phosphopeptides/analysis

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods

KW - Thrombin/metabolism

KW - Titanium/chemistry

U2 - 10.1021/ac902403m

DO - 10.1021/ac902403m

M3 - SCORING: Journal article

C2 - 20067263

VL - 82

SP - 1047

EP - 1053

JO - ANAL CHEM

JF - ANAL CHEM

SN - 0003-2700

IS - 3

M1 - 3

ER -