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High-speed biomarker identification utilizing porous silicon nanovial arrays and MALDI-TOF mass spectrometry

Finnskog, David LU ; Järås, Kerstin LU ; Ressine, Anton LU ; Malm, Johan LU ; Marko-Varga, György LU ; Lilja, Hans LU and Laurell, Thomas LU (2006) In Electrophoresis 27(5-6). p.1093-1103
Abstract
Speed and accuracy are crucial prerequisites in the application of proteomic methods to clinical medicine. We describe a microfluidic-based nanovial array for rapid proteolytic processing linked to MALDI-TOF MS. This microscale format consumes only minute amounts of sample, and it is compatible with rapid bioanalytical protocols and high-sensitivity readouts. Arrays of vials (300 mu m in diameter and 25 mu m deep), isotropically etched in silicon wafers were electrochemically porosified. Automated picoliter microdispensing was employed for precise fluid handling in the microarray format. Vials were prefilled with trypsin solution, which was allowed to dry. Porosified and nonporosified nanovials were compared for trypsin digestion and... (More)
Speed and accuracy are crucial prerequisites in the application of proteomic methods to clinical medicine. We describe a microfluidic-based nanovial array for rapid proteolytic processing linked to MALDI-TOF MS. This microscale format consumes only minute amounts of sample, and it is compatible with rapid bioanalytical protocols and high-sensitivity readouts. Arrays of vials (300 mu m in diameter and 25 mu m deep), isotropically etched in silicon wafers were electrochemically porosified. Automated picoliter microdispensing was employed for precise fluid handling in the microarray format. Vials were prefilled with trypsin solution, which was allowed to dry. Porosified and nonporosified nanovials were compared for trypsin digestion and subsequent MS identification of three model proteins: lysozyme, alcohol dehydrogenase, and serum albumin at levels of 100 and 20 fmol. In an effort to assess the rapid digestion platform in a context of putative clinical applications, two prostate cancer biomarkers, prostate-specific antigen (PSA) and human glandular kallikrein 2 (hK2), were digested at levels of 100 fmol (PSA), 20 fmol (PSA) and 8 fmol (hK2). All biomarker digestions were completed in less than 30 s, with successful MS identification in the porous nanovial setting. (Less)
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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
nanovial arrays, high-speed digestion, MALDI-TOF MS, porous silicon, trypsin digestion
in
Electrophoresis
volume
27
issue
5-6
pages
1093 - 1103
publisher
John Wiley and Sons
external identifiers
  • pmid:16523454
  • wos:000236511900019
  • scopus:33645470650
  • pmid:16523454
ISSN
0173-0835
DOI
10.1002/elps.200500751
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Clinical Chemistry, Malmö (013016000), Biomedical Engineering (011200011), Analytical Chemistry (S/LTH) (011001004)
id
0ac91346-904a-4d43-9401-80dae71a6fbc (old id 414570)
date added to LUP
2016-04-01 12:18:48
date last changed
2021-02-17 05:37:19
@article{0ac91346-904a-4d43-9401-80dae71a6fbc,
  abstract     = {Speed and accuracy are crucial prerequisites in the application of proteomic methods to clinical medicine. We describe a microfluidic-based nanovial array for rapid proteolytic processing linked to MALDI-TOF MS. This microscale format consumes only minute amounts of sample, and it is compatible with rapid bioanalytical protocols and high-sensitivity readouts. Arrays of vials (300 mu m in diameter and 25 mu m deep), isotropically etched in silicon wafers were electrochemically porosified. Automated picoliter microdispensing was employed for precise fluid handling in the microarray format. Vials were prefilled with trypsin solution, which was allowed to dry. Porosified and nonporosified nanovials were compared for trypsin digestion and subsequent MS identification of three model proteins: lysozyme, alcohol dehydrogenase, and serum albumin at levels of 100 and 20 fmol. In an effort to assess the rapid digestion platform in a context of putative clinical applications, two prostate cancer biomarkers, prostate-specific antigen (PSA) and human glandular kallikrein 2 (hK2), were digested at levels of 100 fmol (PSA), 20 fmol (PSA) and 8 fmol (hK2). All biomarker digestions were completed in less than 30 s, with successful MS identification in the porous nanovial setting.},
  author       = {Finnskog, David and Järås, Kerstin and Ressine, Anton and Malm, Johan and Marko-Varga, György and Lilja, Hans and Laurell, Thomas},
  issn         = {0173-0835},
  language     = {eng},
  number       = {5-6},
  pages        = {1093--1103},
  publisher    = {John Wiley and Sons},
  series       = {Electrophoresis},
  title        = {High-speed biomarker identification utilizing porous silicon nanovial arrays and MALDI-TOF mass spectrometry},
  url          = {http://dx.doi.org/10.1002/elps.200500751},
  doi          = {10.1002/elps.200500751},
  volume       = {27},
  year         = {2006},
}