• Mass Spectrometry Letters
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• v.7 no.4
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• pp.91-95
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• 2016

In recent years, matrix-free laser desorption ionization (LDI) for mass spectrometry of thermally labile molecules has been an important research subject in the pursuit of new ionization methods to serve as alternatives to the conventional matrix-assisted laser desorption ionization (MALDI) method. While many recent studies have reported successful LDI of thermally labile molecules from various surfaces, mostly from surfaces with nanostructures, understanding of what drives the LDI process still requires further study. This article briefly reviews the thermal aspects involved in the LDI mechanism, which can be characterized as rapid surface heating. The thermal mechanism was supported by observed LDI and postsource decay (PSD) of peptide ions produced from flat surfaces with special thermal properties including amorphous Si (a-Si) and tungsten silicide ($WSi_x$). In addition, the concept of rapid surface heating further suggests a practical strategy for the preparation of LDI sample plates, which allows us to choose various surface materials including crystalline Si (c-Si) and Au tailorable to specific applications.

• Journal of Photoscience
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• v.8 no.2
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• pp.83-86
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• 2001

Structural analyses of oligosaccharide-malononitrile derivatives were conducted by matrix-assisted laser desorption/ionization post-source decay (MALDI-PSD) analysis in positive ion mode. The malononitrile derivatives of oligosaccharides, which were developed for highly sensitive detection of multi-component oligosaccharides by negative ion electrospray ionization mass spectrometry (ESI MS), were detected by positive-ion MALDI with the detection limit of 2 pmol level from the crude derivatization sample. The used matrix affected drastically the analytical results of oligosaccharide-malononitrile derivative by matrix-assisted laser desoprtion/ionization mass spectrometry (MALDI MS). The malononitrile derivatization of oligosaccharide also affect the patterns of MALDI-PSD spectra and give much more structural information than the free oligosaccharide.

• BMB Reports
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• v.29 no.2
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• pp.122-126
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• 1996

A series of oligonucleotides were synthesized by automatic DNA synthesizer. The purity of crude products was checked and their molecular weights determined by matrix assisted laser desorption ionization mass spectrometry (MALDI-MS) with an accuracy of better than 0.05% deviation even without using an internal standard. This mass determining technology in combination with partial digestion of oligonucleotides by 5'- and 3'-exonuclease provides a straightforward and simple method to obtain sequence information of oligonucleotides. The extension of this technology to the sequencing of modified oligonucleotides and genomic DNA and RNA might become possible.

• Mass Spectrometry Letters
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• v.8 no.4
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• pp.105-108
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• 2017

Recently, deciduous teeth have been proposed as a promising biomatrix for estimating internal and external chemical exposures of an individual from prenatal periods to early childhood. Therefore, detection of organic chemicals in teeth has received increasing attention. Organic materials in tooth matrix are mostly collagen type proteins, but lipids and other small organic chemicals are also present in the tooth matrix. In this study, matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) was employed to obtain lipid fingerprints from deciduous teeth. Phospholipids and triacylglcerols (TAGs) from deciduous teeth were successfully detected by MALDI MS with 2,5-dihydroxybenzoic acid (DHB) or gold nanoparticle (AuNP) as a matrix.

• Mass Spectrometry Letters
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• v.6 no.2
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• pp.27-30
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• 2015

This article reviews the fundamentals of sample preparation used in matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS). MALDI is a soft ionization method used to generate analyte ions in their intact forms, which are then detected in MS analysis. MALDI-MS boasts fast analysis times and easy-to-use operation. The disadvantages of MALDI-MS include the occurrence of matrix-associated peaks and inhomogeneous distribution of analyte within the matrix. To overcome the disadvantages of MALDI-MS, various efforts have been directed such as using different matrices, novel matrix systems, various additives, and different sample preparation methods. These various efforts will be discussed in detail. This article will benefit those who would like to obtain basic knowledge of MALDI sample preparation and those who would like to use MALDI-MS in their chemical analyses.

• Analytical Science and Technology
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• v.8 no.4
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• pp.465-468
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• 1995

Matrix assisted laser desorption ionization in mass spectrometry is a fast and accurate method to determine the molecular weight of natural and synthetic polymers. Unknown peptides such as elastase inhibitor and $\small{D}$-hydantoinase were analyzed using sinapinic acid as matrix and their molecular weights were compared with the results from protein sequencer and gel filtration chomatography, respectively. Synthetic polymers such as polyethyleneglycol, polypropyleneglycol, polydimethylsiloxane, and polystyrene were analyzed using matrices such as 2,5-dihydroxybenzoic acid, 4-hdroxyazobenzenecarboxylic acid, and 2-nitrophenyl octyl ether. Average molecular weights of polystyrene were compared with molecular weights by gel permeation chromatography.

• Analytical Science and Technology
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• v.8 no.4
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• pp.865-868
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• 1995

The method of matrix-assisted laser desorption ionization mass spectrometry has been used to solve some bioanalytical problems, which is difficult to analyse by general methods. For the selection of proper laser wavelength and matrices, eight matriees was used with laser wavelength of 226 and 355nm. The result shows that with wavelength of 355nm better results could be obtained with most of the matrices. The molecular weight of eytochrome C, which was seperated by gel electrophoresis and electro-blotted onto NC membrane is determined by MALDI. The accuracy is better than 0.1%, which is much higher than that of SDS-PAGE. Protein mixture extracted from crude peanut oil is directly determined by MALDI. The molecuiar weight of its three components are determined, and the result also demonstrated that these proteins are in free manner. As proteins arc in 2S bond, with the traditional method, SDS-PAGE, it is not able to decide whether protein exists in combination mode or in free manner. In the technique of two phase aquesous solution, which is used for separating biomaterials, water soluble polymers stained with dyes are used in this technique. By the use of MALDI the number or the dye molecules react with the polymer PEG molecule are determined, and that is difficult to determined by other methods.

• Bulletin of the Korean Chemical Society
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• v.21 no.4
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• pp.401-404
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• 2000

Matrix/Surface-assisted laser desorption/ionization (M/SALDI) mass spectrometry of polypropylene glycol and polystyrene, directly deposited on graphite plate, is demonstrated. Graphite plate is effective both as an en-ergy transfer medium and robu st sampling support for LDI of polymers. Mass spectra ofpolymers can be easily obtained due to homogeneous distribution on graphite surface and their ion signals are long-lived by large ef-fective desorption volume enough to investigate M/SALDI process.

• Bulletin of the Korean Chemical Society
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• v.33 no.3
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• pp.987-992
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• 2012

Magnetic nanoparticles (MNPs) treated with phosphoric acid were used to improve sequence coverage in protein identification by matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). Sample solution of tryptic peptides from proteins was mixed with the MNPs, and the MNPs were separated from the supernatant using a magnet. MALDI mass spectra obtained separately from the supernatant and the MNPs were distinctly different and complementary to each other. Combination of the two spectra led to a significantly increased sequence coverage.

• Mass Spectrometry Letters
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• v.3 no.1
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• pp.18-20
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• 2012

We report observation of laser desorption/ionization (LDI) of peptides from flat surfaces of tungsten silicide ($WSi_2$). In contrast to MALDI (matrix-assisted laser desorption/ionization) and SALDI (surface-assisted laser desorption/ionization) mass spectrometry, this study did not utilize any matrices and surface nanostructures. In this work, LDI on $WSi_2$ surfaces is demonstrated to cover a mass range up to 1,600 Da (somatostatin; monoisotopic mass = 1637.9 Da). In addition, it exhibited a high sensitivity, which could detect peptides, which could detect peptides of low femtomole levels (20 fmol for angiotensin II). The observed LDI process was discussed to be largely thermal, more specifically, due to laser-induced surface heating that is most likely promoted by the low thermal diffusivity (${\kappa}$) of $WSi_2$ substrate.