Novel method for matrix-assisted laser mass spectrometry of proteins

Zhao, Shankai; Somayajula, Kasi V.; Sharkey, A.G.; Hercules, David M.; Hillenkamp, Franz; Karas, Michael; Ingendoh, Arnd

doi:10.1021/ac00005a012

Cited by 85 publications

(31 citation statements)

References 12 publications

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“…Primarily, these are ionic liquid matrices (ILMs) [9,10] and, usually viscous, liquid matrices that are doped with UV light-absorbing chromophores [7,11,12]. However, only a handful of research groups have focused on the further development of liquid MALDI systems and so progress has been slow despite the fact that liquid (UV-and IR-)MALDI was introduced as early as solid MALDI [11,13,14] and liquid MALDI applications and methodologies have been continuously developed since then [15,16].…”

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confidence: 99%

Liquid matrix deposition on conductive hydrophobic surfaces for tuning and quantitation in UV-MALDI mass spectrometry

Palmblad

Cramer

2007

J. Am. Soc. Mass Spectrom.

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With its highly fluctuating ion production matrix-assisted laser desorption/ionization (MALDI) poses many practical challenges for its application in mass spectrometry. Instrument tuning and quantitative ion abundance measurements using ion signal alone depend on a stable ion beam. Liquid MALDI matrices have been shown to be a promising alternative to the commonly used solid matrices. Their application in areas where a stable ion current is essential has been discussed but only limited data have been provided to demonstrate their practical use and advantages in the formation of stable MALDI ion beams. In this article we present experimental data showing high MALDI ion beam stability over more than two orders of magnitude at high analytical sensitivity (low femtomole amount prepared) for quantitative peptide abundance measurements and instrument tuning in a MALDI Q-TOF mass spectrometer. Samples were deposited on an inexpensive conductive hydrophobic surface and shrunk to droplets Ͻ10 nL in size. By using a sample droplet Ͻ10 nL it was possible to acquire data from a single irradiated spot for roughly 10,000 shots with little variation in ion signal intensity at a laser repetition rate of 5-20 Hz. (J Am Soc Mass Spectrom 2007, 18, 693-697)

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confidence: 99%

Liquid matrix deposition on conductive hydrophobic surfaces for tuning and quantitation in UV-MALDI mass spectrometry

Palmblad

Cramer

2007

J. Am. Soc. Mass Spectrom.

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“…Collections of droplets (1,24,50, and 100) prepared by rapid deposition from a methanol solution containing 10 M lysozyme and 0.9% glycerol (Solution II) were analyzed and compared to a sample of the same solution prepared as a 0.5 L dried droplet ( Figure 5). Using the same laser power setting, the ion signals detected from consecutive sets of eight laser shots were averaged to produce the mass spectra shown.…”

Section: The Role Of Multiple Droplet Co-depositionmentioning

confidence: 99%

“…Liquid matrices developed for UV-MALDI have been shown to have some useful characteristics, such as increased shot-toshot reproducibility, but are not commonly used because of adduct formation, relatively poor resolution, and higher detection limits [1][2][3][4][5][6]. Based on their studies of a chemical-doped glycerol matrix that enabled picomole sensitivities for proteins prepared as a 2 L sample spot, Sze et al speculated that the use of smaller matrix droplets and delayed ion extraction could improve the analytical utility of matrix solutions [7].…”

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confidence: 99%

Wall-less sample preparation of μm-sized sample spots for femtomole detection limits of proteins from liquid based UV-MALDI matrices

Bogan

Agnes

2004

J. Am. Soc. Mass Spectrom.

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Previously, we introduced wall-less sample preparation (WaSP), technology that involves the use of an electrodynamic balance (EDB) to prepare m-sized sample spots for analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). In that work we demonstrated the detection of femtomole quantities of a low molecular weight peptide and a hydrophobic ester (both Ͻ600 Da). Here we use WaSP to test the hypothesis that the use of small sample spot sizes and an instrument equipped with delayed extraction would increase the analytical utility of liquid sample spots for peptide and protein (Ͼ2500 Da) analysis by UV-MALDI-TOF-MS (Sze et al.; J. Am. Soc. Mass Spectrom. 1998, 9, 166 -174). To aid the optimization of preparing m-sized sample spots by WaSP, optical microscopy and mass spectrometry were used to investigate nonvolatile solute concentration effects on droplet fission and sample spot size, modifications of the EDB electric field to control droplet ejection, and the use of multiple droplet deposition to increase sample loading. Also described is a rapid deposition mode of operation for WaSP that allows single droplets generated at 1 Hz to be levitated briefly (ϳ500 ms) before being ejected autonomously and deposited as a concentrated sample spot with a spatial accuracy of Ϯ5 m. To test the sensitivity of the method, one hundred glycerol droplets (270 pL each, 27 nL total) each containing 32 amol lysozyme were deposited on top of each other one-at-a-time to create a single sample spot. Using a mass spectrometer equipped with delayed extraction to analyze this sample spot, we verified the hypothesis of Sze et al. by achieving detection limits three orders of magnitude below that previously observed for the detection of a protein by UV-MALDI-TOF-MS with a chemical-doped liquid matrix sample preparation. (J Am Soc Mass Spectrom 2004, 15, 486 -495)

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“…These IMAC materials are often used as surface enhanced laser desorption ionization (Gretzer et al, 2004) and material enhanced laser desorption ionization (MELDI) techniques (Feuerstein et al, 2006;Najam-ul-Haq et al, 2007;Greiderer et al, 2008), especially for protein profiling, screening methods of biological samples and biomarker discovery. The launch of MALDI-MS as a soft ionization method improved the modes of ionization (Rappsilber et al, 2003;Zhao et al, 1991). Much work carried out by MALDI-MS for the investigation of disease biomarkers has been reported (Lehrer et al, 2003;Shahid et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Development of new multifunctional terpolymer sorbent for proteomics applications

Najam‐ul‐Haq

Saeed

Jabeen

et al. 2014

Biomedical Chromatography

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Determination of the availability of phases for specific separations is an important task achieved by a separation chemist. This becomes vital when the complex samples like biofluids are dealt with in proteome science. The work presented here involves the synthesis and application of terpolymeric sorbent with different functionalizations adopted for the selective enrichment of biomolecules of interest from biological fluids. Synthesis of terpolymer was carried out by the radical polymerization of monomers: methyl acrylate, acrylic acid and vinyl acetate with diethylene glycol dimethacrylate as cross-linking agent, benzoyl peroxide as initiator and chloroform as a porogenic solvent. Characterization was done through Fourier transform infrared spectroscopy, scanning electron microscopy and nitrogen adsorption porosimetry. The polymer was further modified to immobilized metal ion affinity chromatographic material, with immobilized Fe(3+)/La(3+) ions that allowed phosphopeptide enrichment from tryptic digests of standard proteins as well as milk, egg yolk and human serum. Sensitivity of enrichment down to 50 fmol was achieved in the presence of complex protein background as bovine serum albumin. Hydrophobicity was introduced through octadecyl amine, which provides comparable results to ZipTip C18/C4 for desalting of complex mixtures of all caseins. Analysis of the enriched content was performed by Matrix Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS).

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Novel method for matrix-assisted laser mass spectrometry of proteins

Cited by 85 publications

References 12 publications

Liquid matrix deposition on conductive hydrophobic surfaces for tuning and quantitation in UV-MALDI mass spectrometry

Liquid matrix deposition on conductive hydrophobic surfaces for tuning and quantitation in UV-MALDI mass spectrometry

Wall-less sample preparation of μm-sized sample spots for femtomole detection limits of proteins from liquid based UV-MALDI matrices

Development of new multifunctional terpolymer sorbent for proteomics applications

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