Integrated Microfluidic System Enabling (Bio)chemical Reactions with On-Line MALDI-TOF Mass Spectrometry

Brivio, Monica; Fokkens, Roel H.; Verboom, Willem; Reinhoudt, David N.; Tas, Niels Roelof; Goedbloed, M.H.; Berg, Albert van den

doi:10.1021/ac020185n

Cited by 105 publications

(83 citation statements)

References 35 publications

(50 reference statements)

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“…A similar concept was explored by Brivio et al [67] using a closed, rather than open, microfluidic chip. Microchannels (200 mm wide and 100 mm deep) were machined by powder blasting into a borosilicate glass substrate.…”

Section: Microfluidic/target Integrationmentioning

confidence: 97%

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Microfluidic technologies for MALDI‐MS in proteomics

DeVoe

Lee

2006

Electrophoresis

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The field of microfluidics continues to offer great promise as an enabling technology for advanced analytical tools. For biomolecular analysis, there is often a critical need to couple on-chip microfluidic sample manipulation with back-end MS. Though interfacing microfluidics to MS has been most often reported through the use of direct ESI-MS, there are compelling reasons for coupling microfluidics to MALDI-MS as an alternative to ESI-MS for both online and offline analysis. The intent of this review is to provide a summary of recent developments in the integration of microfluidic systems with MALDI-MS, with an emphasis on applications in proteomics. Key points are summarized, followed by a review of relevant technologies and a discussion of outlook for the field.

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Section: Microfluidic/target Integrationmentioning

confidence: 97%

“…Photograph of a vacuum-driven microfluidic reaction chip containing an open exit reservoir for MALDI laser access. The glass chip is integrated with into a standard MALDI plate [67].…”

Section: Microfluidic/target Integrationmentioning

confidence: 99%

Microfluidic technologies for MALDI‐MS in proteomics

DeVoe

Lee

2006

Electrophoresis

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“…Most approaches focused on biological MS integrated to microfluidic chips employ ESI [11][12][13][14][15][16][17][18] and only a few have used MALDI [19,20]. Although ESI and MALDI are often complimentary techniques, the preference of ESI interfaces between microchips and MS can be explained by the fundamentals behind the two ionization methods.…”

Section: Introductionmentioning

confidence: 99%

“…A continuous pressure driven self-activating flow on-chip microfluidic device connected to MALDI-TOF mass spectrometer has also been reported [20]. The integration was achieved by placing the microdevice on a standard MALDI sample plate, which had a rectangular hole milled to fit the entire device.…”

Section: Introductionmentioning

confidence: 99%

Direct coupling of polymer-based microchip electrophoresis to online MALDI-MS using a rotating ball inlet

et al. 2005

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We report on the coupling of a polymer-based microfluidic chip to a MALDI-TOF MS using a rotating ball interface. The microfluidic chips were fabricated by micromilling a mold insert into a brass plate, which was then used for replicating polymer microparts via hot embossing. Assembly of the chip was accomplished by thermally annealing a cover slip to the embossed substrate to enclose the channels. The linear separation channel was 50 microm wide, 100 microm deep, and possessed an 8 cm effective length separation channel with a double-T injector (V(inj) = 10 nL). The exit of the separation channel was machined to allow direct contact deposition of effluent onto a specially constructed rotating ball inlet to the mass spectrometer. Matrix addition was accomplished in-line on the surface of the ball. The coupling utilized the ball as the cathode transfer electrode to transport sample into the vacuum for desorption with a 355 nm Nd:YAG laser and analyzed on a TOF mass spectrometer. The ball was cleaned online after every rotation. The ability to couple poly(methylmethacrylate) microchip electrophoresis devices for the separation of peptides and peptide fragments produced from a protein digest with subsequent online MALDI MS detection was demonstrated.

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“…In other off-line approaches, the sample is dispensed from the chip using a piezoelectric dispenser [25], pumped through a spinning microfluidic disk [26], or sample droplets moved on a dielectric chip surface by electrowetting [27,28]. In a unique on-line approach, the vacuum of the mass spectrometer source is used to pull fluid through a microfluidic chip where it is subjected to UV MALDI as it exits the device [29,30]. A second on-line approach uses a rotating stainless steel ball coupled to an on-chip capillary electrophoresis for the separation of peptides [31].…”

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confidence: 99%

Interfacing capillary gel microfluidic chips with infrared laser desorption mass spectrometry

Little

Murray

2006

J. Am. Soc. Mass Spectrom.

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We report on the fabrication and performance of a gel microfluidic chip interfaced to laser desorption/ionization (LDI) mass spectrometry with a time-of-flight mass analyzer. The chip was fabricated from poly(methylmethacrylate) with a poly(dimethyl siloxane) cover. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed in the channel of the microfluidic chip. After electrophoresis, the cover was removed and either the PDMS chip or the PMMA cover was mounted in a modified MALDI ion source for analysis. Ions were formed by irradiating the channel with 2.95 m radiation from a pulsed optical parametric oscillator (OPO), which is coincident with IR absorption by N-H and O-H stretch of the gel components. No matrix was added. The microfluidic chip design allowed a decrease in the volume of material required for analysis over conventional gel slabs, thus enabling improvement in the detection limit to a pmol level, a three orders of magnitude improvement over previous studies in which desorption was achieved from an excised section of a conventional gel. ( T he rapid expansion of the field of proteomics has created an increased demand for selective, sensitive, and high-throughput methods of analysis. Soft ionization methods, such as matrix-assisted desorption/ionization (MALDI) [1,2] and electrospray (ESI) [3,4] are suitable for achieving the goal of identification and structural determination of proteins. Mass spectrometry (MS) has become the primary analysis method in this area because of its high throughput, sensitivity, and high mass accuracy. However, the large number and broad concentration range of the proteins present in the expressed proteome of a typical organism requires that one or more fractionation or separation steps be performed on the sample before mass spectrometry analysis.One of the most commonly utilized techniques for protein separation is sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) [5][6][7][8][9]. The molecular weight of a protein is determined by the migration distance after electrophoretic separation together with several marker proteins of known molecular weights that bracket the protein of interest. Currently, most proteome analyses are based on the separation of complex protein mixtures by 1D or 2D gel electrophoresis, followed by mass spectrometric analysis of proteolytic digests of gel spots to identify individual proteins [10 -13]. However, this protocol requires intermediate sample processing steps such as extraction of the protein from the gel [13], blotting the protein onto a membrane [14], or electroelution [15], which introduces a number of laborious and time-consuming manual steps that are difficult to automate.Various efforts have been directed toward direct analysis of gel and planar chromatography separations by laser desorption ionization (LDI) mass spectrometry. The mass spectrometric analysis of peptides and proteins by UV-MALDI directly from polyacrylamide gels has been reported previously [16]. Here, ultrathin gels (less than 10 m) ...

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Integrated Microfluidic System Enabling (Bio)chemical Reactions with On-Line MALDI-TOF Mass Spectrometry

Cited by 105 publications

References 35 publications

Microfluidic technologies for MALDI‐MS in proteomics

Microfluidic technologies for MALDI‐MS in proteomics

Direct coupling of polymer-based microchip electrophoresis to online MALDI-MS using a rotating ball inlet

Interfacing capillary gel microfluidic chips with infrared laser desorption mass spectrometry

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