Matrix-assisted laser-desorption ionization possibilities

Two relatively new techniques, matrix assisted laser desorption ionization-lime of flight mass spectrometry (MALDI-TOF) and electrospray ionization (FS1), offer new possibilities for analysis of polymers with molecular weights in the tens of thousands. PS molecular weights as high as 1.5 million have been determined by MALDI-TOF. Recent reviews on the application of these techniques to synthetic polymers include those by Ilantoif54 and Nielen.555 The methods have been much used to provide evidence for initiation and termination mechanisms in various forms of living and controlled radical polymerization.550 Some examples of the application of MALDI-TOF and ESI in end group determination are provided in Table 3.12. The table is not intended to be a comprehensive survey. 

The second advantage is the possibility of performing chemical imaging analyses. Even if other techniques, such as matrix-assisted laser desorption/ionization, also allow images to be acquired, ToF-SIMS is, for now, the mass spectrometric technique with the best spatial resolution performance. 

There are at least three possibile ways in which the inhibitor can bind to the active site (1) formation of a sulfide bond to a cysteine residue, with elimination of hydrogen bromide [Eq. (10)], (2) formation of a thiol ester bond with a cysteine residue at the active site [Eq. (11)], and (3) formation of a salt between the carboxyl group of the inhibitor and some basic side chain of the enzyme [Eq. (12)]. To distinguish between these three possibilities, the mass numbers of the enzyme and enzyme-inhibitor complex were measured with matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI). The mass number of the native AMDase was observed as 24766, which is in good agreement with the calculated value, 24734. An aqueous solution of a-bromo-phenylacetic acid was added to the enzyme solution, and the mass spectrum of the complex was measured after 10 minutes. The peak is observed at mass number 24967. If the inhibitor and the enzyme bind to form a sulfide with elimination of HBr, the mass number should be 24868, which is smaller by about one... 

In the last years, ILs have been applied as matrices for matrix-assisted laser desorption/ionization (MALDI) MS [42], thus expanding the use of MALDI. In Ref. 38 the suitability of alkylammonium- and alkylimidazolium salts of a-cyano-4-hydroxycinnamic acid was investigated as a MALDI matrix and at the same time as the additive of BGE. The alkylammonium salt produced better separation of phenolic compounds than the alkylimidazolium salt. The investigation suggests that it is possible to synthesize ILs suitable for electrophoretic analysis as well as for online MALDI-MS analysis. 

Finally, another method commonly used to characterize these copolymeric materials is that of matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry. When using this technique, it is possible to investigate the molecular weight distributions, end groups, and polymer constitution of low-molecular-weight samples [63], MALDI-TOF may also provide vital... 

MS has become an indispensable tool for the determination of carbohydrate structures. The information provided by this methodology ranges from accurate molecular weight determination to the complete primary structure, with picomole sensitivity. These remarkable advances have been possible because of the development of novel methods of ionization, such as fast atom bombardment (FAB) ionization, ESI, and matrix-assisted laser desorption/ionization (MALDI) (Fig. 3). 

Developments in mass spectrometry technology, together with the availability of extensive DNA and protein sequence databases and software tools for data mining, has made possible rapid and sensitive mass spectrometry-based procedures for protein identification. Two basic types of mass spectrometers are commonly used for this purpose Matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF) mass spectrometry (MS) and electrospray ionization (ESI)-MS. MALDI-TOF instruments are now quite common in biochemistry laboratories and are very simple to use, requiring no special training. ESI instruments, usually coupled to capillary/nanoLC systems, are more complex and require expert operators. We will therefore focus on the use of MALDI-... 

Mass spectrometry has been used to determine the molecular weight of small labile molecules precisely. The analysis of macromolecules became possible following the development of novel mass spectrometry technologies, especially, Matrix-assisted laser desorption ionization time of flight mass... 

Development of a wide range of Surface MALDI mass spectrometry methods12 opens new possibilities in MS investigations of bio-interfacial phenomena, summarized recently as biological surface science . Thus, matrix-assisted laser desorption ionization mass spectrometry, and its variants, hold promise to help clarify the mechanisms of bio-activity of silica-based nanocomposites. 

The use of mass spectrometry (MS) techniques to monitor SP reactions has recently become possible through the use of matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) spectrometry (137) after in situ cleavage of a small number of resin beads (138-140). Although the compound is cleaved from the resin, the cleavage happens directly onto the center of the MALDI target and the method can be considered on-bead. 

Elaboration of nerve agent toxicokinetics requires sophisticated analytical tools to detect and, if possible, to quantify the free toxicants as well as adducts with proteins and enzymes. Analysis of OP nerve agents has been performed by capillary electrophoresis (CE), biosensors, matrix-assisted laser desorption/ionization (MALDI) MS, desorption electrospray ionization MS (DESI MS), ion mobility time-of-flight MS (IM-TOF MS), nuclear magnetic resonance spectroscopy (NMR), LC-UV, gas chromatography (GC), and many more techniques (Hooijschuur et al, 2002 John et al, 2008). 

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