A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis

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A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis. / Lu, Nan; Sticker, Drago; Kretschmann, Andreas; Petersen, Nickolaj J; Kutter, Jörg P.

In: Analytical and Bioanalytical Chemistry, Vol. 412, No. 15, 06.2020, p. 3559-3571.

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

Harvard

Lu, N, Sticker, D, Kretschmann, A, Petersen, NJ & Kutter, JP 2020, 'A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis', Analytical and Bioanalytical Chemistry, vol. 412, no. 15, pp. 3559-3571. https://doi.org/10.1007/s00216-020-02609-5

APA

Lu, N., Sticker, D., Kretschmann, A., Petersen, N. J., & Kutter, J. P. (2020). A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis. Analytical and Bioanalytical Chemistry, 412(15), 3559-3571. https://doi.org/10.1007/s00216-020-02609-5

Vancouver

Lu N, Sticker D, Kretschmann A, Petersen NJ, Kutter JP. A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis. Analytical and Bioanalytical Chemistry. 2020 Jun;412(15):3559-3571. https://doi.org/10.1007/s00216-020-02609-5

Author

Lu, Nan ; Sticker, Drago ; Kretschmann, Andreas ; Petersen, Nickolaj J ; Kutter, Jörg P. / A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis. In: Analytical and Bioanalytical Chemistry. 2020 ; Vol. 412, No. 15. pp. 3559-3571.

Bibtex

@article{e4be4f433c7c418486657303424118f4,
title = "A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis",
abstract = "One of the most attractive aspects of microfluidic chips is their capability of integrating several functional units into one single platform. In particular, enzymatic digestion and chemical separation are important steps in processing samples for many biochemical assays. This study presents the development and application of a free-flow electrophoresis microfluidic chip, and its upstream combination with an enzyme microreactor with immobilized pepsin in the same miniaturized platform. The whole microfluidic chip was fabricated by making use of thiol-ene click chemistry. As a proof of concept, different fluorescent dyes and labeled amino acids were continuously separated in the 2D electrophoretic channel. The protease pepsin was immobilized using a covalent linkage with ascorbic acid onto a high-surface monolithic support, also made of thiol-ene. To show the potential of the microfluidic chip for continuous sample preparation and analysis, an oligopeptide was enzymatically digested, and the resulting fragments were separated and collected in a single step (prior to mass spectrometric detection), without the need of further time-consuming liquid handling steps.",
author = "Nan Lu and Drago Sticker and Andreas Kretschmann and Petersen, {Nickolaj J} and Kutter, {J{\"o}rg P}",
year = "2020",
month = jun,
doi = "10.1007/s00216-020-02609-5",
language = "English",
volume = "412",
pages = "3559--3571",
journal = "Analytical and Bioanalytical Chemistry",
issn = "1618-2642",
publisher = "Springer",
number = "15",

}

RIS

TY - JOUR

T1 - A thiol-ene microfluidic device enabling continuous enzymatic digestion and electrophoretic separation as front-end to mass spectrometric peptide analysis

AU - Lu, Nan

AU - Sticker, Drago

AU - Kretschmann, Andreas

AU - Petersen, Nickolaj J

AU - Kutter, Jörg P

PY - 2020/6

Y1 - 2020/6

N2 - One of the most attractive aspects of microfluidic chips is their capability of integrating several functional units into one single platform. In particular, enzymatic digestion and chemical separation are important steps in processing samples for many biochemical assays. This study presents the development and application of a free-flow electrophoresis microfluidic chip, and its upstream combination with an enzyme microreactor with immobilized pepsin in the same miniaturized platform. The whole microfluidic chip was fabricated by making use of thiol-ene click chemistry. As a proof of concept, different fluorescent dyes and labeled amino acids were continuously separated in the 2D electrophoretic channel. The protease pepsin was immobilized using a covalent linkage with ascorbic acid onto a high-surface monolithic support, also made of thiol-ene. To show the potential of the microfluidic chip for continuous sample preparation and analysis, an oligopeptide was enzymatically digested, and the resulting fragments were separated and collected in a single step (prior to mass spectrometric detection), without the need of further time-consuming liquid handling steps.

AB - One of the most attractive aspects of microfluidic chips is their capability of integrating several functional units into one single platform. In particular, enzymatic digestion and chemical separation are important steps in processing samples for many biochemical assays. This study presents the development and application of a free-flow electrophoresis microfluidic chip, and its upstream combination with an enzyme microreactor with immobilized pepsin in the same miniaturized platform. The whole microfluidic chip was fabricated by making use of thiol-ene click chemistry. As a proof of concept, different fluorescent dyes and labeled amino acids were continuously separated in the 2D electrophoretic channel. The protease pepsin was immobilized using a covalent linkage with ascorbic acid onto a high-surface monolithic support, also made of thiol-ene. To show the potential of the microfluidic chip for continuous sample preparation and analysis, an oligopeptide was enzymatically digested, and the resulting fragments were separated and collected in a single step (prior to mass spectrometric detection), without the need of further time-consuming liquid handling steps.

U2 - 10.1007/s00216-020-02609-5

DO - 10.1007/s00216-020-02609-5

M3 - Journal article

C2 - 32253474

VL - 412

SP - 3559

EP - 3571

JO - Analytical and Bioanalytical Chemistry

JF - Analytical and Bioanalytical Chemistry

SN - 1618-2642

IS - 15

ER -

ID: 245617280