Laser desorption-mass spectrometry of polar nonvolatile bio-organic molecules

Posthumus, M.A.; Kistemaker, Piet G.; Meuzelaar, Henk L. C.; Brauw, M.C. ten Noever de

doi:10.1021/ac50029a040

Cited by 443 publications

(94 citation statements)

References 38 publications

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“…For oligopeptides, MS can utilize picomole samples, determine exact molecular weights, identify unusual amino acids or terminal groups (1)(2)(3)(4), and detect frameshift errors in Maxam-Gilbert sequencing of the gene encoding an enzyme (5). MS characterization of larger peptides is now possible by using powerful methods for the ionization of nonvolatile molecules, such as fast atom bombardment (FAB) (2,(6)(7)(8)(9)(10), laser desorption (LD) (11)(12)(13)(14), and particle-induced desorption (15,16). The latter has recently been used to measure molecular ions of 23,406 ± 140 daltons from porcine trypsin (16).…”

mentioning

confidence: 99%

Peptide mixture sequencing by tandem Fourier-transform mass spectrometry.

Cody¹,

Amster²,

McLafferty³

1985

Proc. Natl. Acad. Sci. U.S.A.

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Picomole samples of the linear peptide gramicidin D and cyclic peptide gramicidin S are shown to be impure by the laser-desorption formation of multiple groups of molecular adduct peaks by using Fourier-transform mass spectrometry. Selective excitation of the molecular peaks of the major sample component followed by collisionally activated dissociation provides complete sequence information for the cyclic decapeptide and for 12 of the 15 amino acids of the linear peptide. This instrumentation shows striking advantages in sensitivity, resolution, and mass accuracy in comparison to tandem mass spectrometers used previously.Mass spectrometry (MS) provides information complementary to conventional techniques for the molecular characterization of peptides and other important macromolecules (1-3). For oligopeptides, MS can utilize picomole samples, determine exact molecular weights, identify unusual amino acids or terminal groups (1-4), and detect frameshift errors in Maxam-Gilbert sequencing of the gene encoding an enzyme (5). MS characterization of larger peptides is now possible by using powerful methods for the ionization of nonvolatile molecules, such as fast atom bombardment (FAB) (2, 6-10), laser desorption (LD) (11-14), and particle-induced desorption (15, 16). The latter has recently been used to measure molecular ions of 23,406 ± 140 daltons from porcine trypsin (16). However, sequence information for larger peptides is often limited by the small degree of fragmentation observed (6-8, 11-13, 15, 16) and by misleading fragments arising from impurities; sample purity is also a critical limitation in conventional methods of peptide sequencing. Tandem mass spectrometry (MS/MS) offers a possible solution to both problems (17,25,26,30). In MS/MS the molecular ion species of a mixture component can be separated by MS-I, fragmented by collisionally activated dissociation (CAD) (17) or laser photodissociation (18,19) to produce fragments measured in MS-II indicating the peptide sequence (7, 8, 17-21, 25, 26, 30).However, the few examples in which MS/MS has been applied to larger peptides (ionized by FAB) gave only limited sequence information of poor resolution (peak widths, >3 daltons), sensitivity (nmol samples), and mass accuracy (7,8,17,25,26). This arises because primary ion dissociations are accompanied by translational energy release, causing both broadening and shifting of peaks in magnetic sector instruments (17). Fourier-transform mass spectrometry (FTMS) (22-24) offers a promising alternative for such studies. The measured cyclotron frequency only depends on the magnetic field and ion's mass, not on its translational energy. Further, the masses of nearly all (e.g., m/z 100-16,000, broad-band recording) ions can be measured simultaneously, so that pulsed ionization is feasible; scanning instruments require continuous ionization, at any instant wasting all ions formed except those of the exact mass measured. For modem FTMS instrumentation we have recently demonstrated high (>16,000) mass range and ...

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mentioning

confidence: 99%

Peptide mixture sequencing by tandem Fourier-transform mass spectrometry.

Cody¹,

Amster²,

McLafferty³

1985

Proc. Natl. Acad. Sci. U.S.A.

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“…Taking into account the pioneering works of several research groups in the early 1980s [1][2][3][4][5][6][7][8][9], which investigated direct laser desorption/ionization of organic materials, we first tried to analyze our peptide samples without any substrate by depositing the peptide solution directly on the stainless steel MALDI plate. The results were very promising in terms of sensitivity and detection mass range but the low mass part of the spectra was exhibiting a lot of signals ( Figure 3).…”

Section: Preliminary Ldi Analysesmentioning

confidence: 99%

“…The results gathered from synthetic peptide cocktails indicated that LDI mass spectrometry on silica gel or alumina constitutes a promising complementary method to MALDI in proteomics for peptide mass fingerprinting. [1][2][3][4][5][6][7][8][9] was investigated by Siuzdak and collaborators using porous silicon as the substrate [10]. This desorption/ionization on porous silicon (DIOS) mass spectrometry [10] allows the analysis of various compounds, such as small organic molecules [11], amino acids [12], peptides [13], and fatty acids [14].…”

mentioning

confidence: 99%

Laser desorption/ionization mass spectrometry on porous silica and alumina for peptide mass fingerprinting

Shenar

Martinez

Enjalbal

2008

J. Am. Soc. Mass Spectrom.

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We investigated a variant of desorption/ionization on porous silicon (DIOS) mass spectrometry utilizing an aqueous suspension of either porous silica gel or porous alumina (pore size of 60 and 90 Å, respectively). Laser desorption/ionization (LDI) from samples directly deposited on a stainless steel surface without any inorganic substrates was also achieved. Synthetic peptides designed to cover large sequence diversity constituted our model compounds. Sample preparation, including material conditioning, peptide solubilization, and deposition protocol onto standard matrix-assisted laser desorption/ionization (MALDI) probe, as well as ionization source tuning were optimized to perform sensitive reproducible LDI analyses. The addition of either a cationizing agent or an alkali metal scavenger to the sample suspension allowed modification of the ionization output. Comparing hydrophilic silica gel to hydrophobic reversed-phase silica gel as well as increasing material pore size provided further insights into desorption/ionization processes. Furthermore, mixtures of peptides were analyzed to probe the spectral suppression phenomenon when no interfering organic matrix was present. The results gathered from synthetic peptide cocktails indicated that LDI mass spectrometry on silica gel or alumina constitutes a promising complementary method to MALDI in proteomics for peptide mass fingerprinting. [19]. These LDI methods, sometimes referred to as "matrix-free", produce mass spectra that exhibit less matrix ions in the low mass range compared with the chemical noise generated by the organic matrices used in matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. Such chemical noise that usually pollutes the low mass range of MALDI mass spectra and that may complicate the detection of small molecules is less pronounced in the DIOS mass spectra.Nevertheless, the drawback of such an approach is in the preparation of the silicon material. To present adequate physical properties [20], silicon surfaces are conditioned via a galvanostatic etching procedure from Si wafer to produce pores with nanometer diameters. Commercially available ready-to-use DIOS-chips can also be mounted on modified MALDI plates [20]. Otherwise, silicon powders (5 to 50 nm particle size) were investigated as a substitute to DIOS chips to make the overall sample preparation simpler and safer [18]. Provided that the appropriate powder preparation was performed (including particle etching by HF, oxidation by HNO 3 , and derivatization of the generated SiOH groups), such silicon nanopowder method was found to exhibit the same characteristics as DIOS mass spectrometry.Porous silicon is a material that presents (1) a large active surface and (2) a strong absorbance in the UV range. Such a form of silicon was thus found particularly suitable for LDI mass spectrometry with irradiation at 337 nm, the pore size and the surface chemical nature being the most important parameters as stated by Siuzdak and coworkers in their early publications on DIOS [20...

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“…The process of elucidating the mass and the structure of a substance can be expedited by using a high performance mass spectrometer. With the advent of "soft" ionization mass spectrometric techniques such as plasma desorption (PD) 4 , laser desorption (LD) 5 , and electrospray ionization (ESI) 6 that produce protonated molecular ions with minimal or no fragmentation, pseudo-molecular ions of each eluting species can be readily produced. The ESI mass spectrometry 6 is superior to others in this respect since structurally significant information can be elicited by collisional activation of the eluting species in the vacuum interface of the ESI source.…”

Section: Introductionmentioning

confidence: 99%

Application of mass pectrometry to characterize the components present in curcumin Sample

Coorey

Håkansson

2003

Sri Lankan J Phys

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The identification of the components present in crude samples purely by mass spectrometric techniques has been a long-standing problem. Conventionally, components present in a crude sample are isolated and purified by chromatographic methods and then various spectrometric techniques (including mass spectrometric techniques) are adopted for their structure elucidation and physical characterization. This paper gives an example illustrating the characterization of the components present in a crude sample purely by mass spectrometric techniques.A commercially obtained curcumin sample (Assay: 65-70%) was chosen for this purpose. The mass analysis of this sample using time-of-flight reflectron mass spectrometric techniques namely plasma desorption (PD), laser desorption (LD) and electrospray ionization (ESI) gave evidence for the presence of curcuminoids other than curcumin in the sample. The electrospray Fourier transform ionization cyclotron resonance mass spectrometry combined with tandem mass spectrometry (MS/MS) has been adopted successfully to confirm the presence of all curcuminoids in the curcumin sample.

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Laser desorption-mass spectrometry of polar nonvolatile bio-organic molecules

Cited by 443 publications

References 38 publications

Peptide mixture sequencing by tandem Fourier-transform mass spectrometry.

Peptide mixture sequencing by tandem Fourier-transform mass spectrometry.

Laser desorption/ionization mass spectrometry on porous silica and alumina for peptide mass fingerprinting

Application of mass pectrometry to characterize the components present in curcumin Sample

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