Application Of Matrix-assisted Laser Desorption Ionization Research Articles

Nanomaterials as Assisted Matrix of Laser Desorption/Ionization Time-of-Flight Mass Spectrometry for the Analysis of Small Molecules.

Matrix-assisted laser desorption/ionization (MALDI), a soft ionization method, coupling with time-of-flight mass spectrometry (TOF MS) has become an indispensible tool for analyzing macromolecules, such as peptides, proteins, nucleic acids and polymers. However, the application of MALDI for the analysis of small molecules (<700 Da) has become the great challenge because of the interference from the conventional matrix in low mass region. To overcome this drawback, more attention has been paid to explore interference-free methods in the past decade. The technique of applying nanomaterials as matrix of laser desorption/ionization (LDI), also called nanomaterial-assisted laser desorption/ionization (nanomaterial-assisted LDI), has attracted considerable attention in the analysis of low-molecular weight compounds in TOF MS. This review mainly summarized the applications of different types of nanomaterials including carbon-based, metal-based and metal-organic frameworks as assisted matrices for LDI in the analysis of small biological molecules, environmental pollutants and other low-molecular weight compounds.

Application of MALDI TOF/TOF mass spectrometry and collision‐induced dissociation for the identification of disulfide‐bonded peptides

This paper describes a method for the fast identification and composition of disulfide-bonded peptides. A unique fragmentation signature of inter-disulfide-bonded peptides is detected using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF)/TOF mass spectrometry and high-energy collision-induced dissociation (CID). This fragmentation pattern identifies peptides with an interconnected disulfide bond and provides information regarding the composition of the peptides involved in the pairing. The distinctive signature produced using CID is a triplet of ions resulting from the cleavage of the disulfide bond to produce dehydroalanine, cysteine or thiocysteine product ions. This method is not applicable to intra-peptide disulfide bonds, as the cleavage mechanism is not the same and a triplet pattern is not observed. This method has been successfully applied to identifying disulfide-bonded peptides in a number of control digestions, as well as study samples where disulfide bond networks were postulated and/or unknown.

Metabolic profiling of Escherichia coli by ion mobility-mass spectrometry with MALDI ion source.

Comprehensive metabolome analysis using mass spectrometry (MS) often results in a complex mass spectrum and difficult data analysis resulting from the signals of numerous small molecules in the metabolome. In addition, MS alone has difficulty measuring isobars and chiral, conformational and structural isomers. When a matrix-assisted laser desorption ionization (MALDI) source is added, the difficulty and complexity are further increased. Signal interference between analyte signals and matrix ion signals produced by MALDI in the low mass region (<1500 Da) cause detection and/or identification of metabolites difficult by MS alone. However, ion mobility spectrometry (IMS) coupled with MS (IM-MS) provides a rapid analytical tool for measuring subtle structural differences in chemicals. IMS separates gas-phase ions based on their size-to-charge ratio. This study, for the first time, reports the application of MALDI to the measurement of small molecules in a biological matrix by ion mobility-time of flight mass spectrometry (IM-TOFMS) and demonstrates the advantage of ion-signal dispersion in the second dimension. Qualitative comparisons between metabolic profiling of the Escherichia coli metabolome by MALDI-TOFMS, MALDI-IM-TOFMS and electrospray ionization (ESI)-IM-TOFMS are reported. Results demonstrate that mobility separation prior to mass analysis increases peak-capacity through added dimensionality in measurement. Mobility separation also allows detection of metabolites in the matrix-ion dominated low-mass range (m/z < 1500 Da) by separating matrix signals from non-matrix signals in mobility space.

Developments in MALDI Mass Spectrometry: The Quest for the Perfect Matrix

The topic of matrix-assisted laser desorption/ionization (MALDI) mass spectrometry has received much attention over the past several years and with the award of the Nobel Prize to Tanaka based on his landmark paper in 1988, has received even more recent attention. This review focuses on the search for an ideal matrix and generally covers the period from the mid 1990's to the present. There have been a number of excellent and comprehensive reviews on MALDI ion formation and a brief summary of some of the most important conclusions is given here. With respect to the applications of MALDI, the present review focuses primarily on polymer analysis, although in this area too, excellent reviews have been published that include consideration of the MALDI method. Although we make some mention of other uses of MALDI (e.g., to proteins and peptides) and other biological applications, we emphasize the polymer uses in the present review.

4-Chloro-α-cyanocinnamic acid is an advanced, rationally designed MALDI matrix

Matrix-assisted laser desorption ionization (MALDI) has become an enabling technology for the fields of protein mass spectrometry (MS) and proteomics. Despite its widespread use, for example, in protein identification via peptide mass fingerprinting, a comprehensive model for the generation of free gas-phase ions has not yet been developed. All matrices in use today, such as alpha-cyano-4-hydroxycinnamic acid (CHCA), have been found empirically and stem from the early days of MALDI. By systematic and targeted variation of the functional groups of the alpha-cyanocinnamic acid core unit, 4-chloro-alpha-cyanocinnamic acid (Cl-CCA) was selected and synthesized, and it exhibited outstanding matrix properties. Key features are a substantial increase in sensitivity and a considerably enhanced peptide recovery in proteomic analyses because of a much more uniform response to peptides of different basicity. Using Cl-CCA as a matrix for a 1 fmol bovine serum albumin (BSA) in-solution digest, the sequence coverage is raised to 48%, compared with 4% for CHCA. For a gel band containing 25 fmol of BSA, unambiguous protein identification becomes possible with Cl-CCA. These findings also imply ion formation via a chemical ionization mechanism with proton transfer from a reactive protonated matrix species to the peptide analytes. The considerable increase in performance promises to have a strong impact on future analytical applications of MALDI, because current sensitivity limits are overcome and more comprehensive analyses come into reach.

Fractionation and Solvent-Free MALDI-MS Analysis of Polymers Using Liquid Adsorption Chromatography at Critical Conditions in Combination with a Multisample On-Target Homogenization/Transfer Sample Preparation Method

A solvent-free homogenization/transfer matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) method is described for the preparation and precise transfer of up to 100 samples simultaneously on a single MALDI plate. This method is demonstrated using a poly(ethylene oxide) (PEO) mixture consisting of different molecular weights (500-6000) and end groups (PEO, dimethoxy-PEO, monomethoxy monomethacrylate-PEO, and dimethacrylate-PEO) that was fractionated using liquid adsorption chromatography at critical conditions. Off-line fractionation is performed prior to the on-target homogenization/transfer solvent-free sample preparation and MALDI mass analysis. The miniaturization of the solvent-free MALDI approach allowed analysis of less than 2 microg per PEO component per fraction corresponding to approximately 200 pmol for PEO 6000. The amounts of polymer sample used for LC separation and the quality of the MS results are equivalent to the "dry spray" method; however, three times more fractions were collected and analyzed with the newly developed hyphenated approach. The off-line method eliminates optimization of, for example, spray conditions or spreading of organic solvents on the MALDI plate that occurs with droplet deposition methods. The widespread applications of MALDI make this solvent-free, multisample method particularly important as it expands the capabilities for obtaining mass measurements with great efficiencies in areas with increased sample numbers. In addition, the solvent-free method is well suited for automated MALDI analysis as it virtually eliminates the "dead-spot" phenomenon.

Current Trends in Matrix-Assisted Laser Desorption/Ionization of Polymeric Materials

In the last few years, mass spectrometry has rapidly become indispensable in polymer analysis and complements, in many ways, the structural data provided by nuclear magnetic resonance. Mass spectrometry of polymers is emerging as a revolutionary technique, capable of challenging the techniques and protocols established for years for the characterization of synthetic polymers. Matrix-assisted laser desorption/ionization (MALDI) has become a widely applied method for the structural characterization of synthetic polymers. The primary aim of this review is to illustrate some recent advances in the study of macromolecular systems by MALDI. MALDI allows the identification of repeat units and end groups, the structural analysis of linear and cyclic oligomers and the estimate of composition and sequence for co-polymers. MALDI is also quite useful for the measurement of molar mass and bivariate distributions in polymers and for the detection of self-association in macromolecules, performed by coupling MALDI with size exclusion chromatography (SEC). Recently MALDI has been applied, with remarkable success, to the study of thermal and oxidative processes in polymers and to the characterization of co-polymers obtained by reactive polymer blending. Selected applications of MALDI to polymers are illustrated herewith.

Matrix‐Assisted Laser Desorption/Ionization Mass Spectrometry of Carbohydrates and Glycoconjugates

AbstractFor Abstract see ChemInform Abstract in Full Text.

MALDI for fast DNA analysis and sequencing

Matrix-assisted laser desorption/ionization (MALDI) has been pursued for fast DNA analysis and sequencing. In this article, recent progress on detecting large oligonucleotides is reviewed. The potential application of MALDI for population screening for disease diagnosis is discussed. The approach of using MALDI for DNA sequencing is presented. Discussion on the use of robotic and automation to speed up the mass spectrometer sequencing process is also included. © 1996 John Wiley & Sons, Inc.

Mass spectrometry of nucleic acids: the promise of matrix-assisted laser desorption-ionization (MALDI) mass spectrometry.

In the past several years, significant progress has been made in the application of matrix-assisted laser desorption-ionization (MALDI) mass spectrometry to the analysis of large biopolymers, including nucleic acids. By isolating analyte molecules in an appropriate matrix and irradiating the sample with a high-intensity, pulsed laser beam, MALDI can generate intact, gas-phase ions of these analytes. Primarily used with time-of-flight mass spectrometers, this relatively new, soft ionization technique has allowed for the routine analysis of oligonucleotides up to 60 or so nucleotides in length. Recent results have also shown that base specific, matrix-dependent fragmentation is an important factor in the MALDI analysis of oligonucleotides. Further extension of the technique to longer oligonucleotides will rely on both the continued search for new matrix materials and an increased understanding of the desorption and ionization process in MALDI.

The emergence of mass spectrometry in biochemical research.

The initial steps toward routinely applying mass spectrometry in the biochemical laboratory have been achieved. In the past, mass spectrometry was confined to the realm of small, relatively stable molecules; large or thermally labile molecules did not survive the desorption and ionization processes intact. Electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry allow for the analysis of both small and large biomolecules through "mild" desorption and ionization methods. The use of ESI and MALDI mass spectrometry extends beyond simple characterization. Noncovalent interactions, protein and peptide sequencing, DNA sequencing, protein folding, in vitro drug analysis, and drug discovery are among the areas to which ESI and MALDI mass spectrometry have been applied. This review summarizes recent developments and major contributions in mass spectrometry, focusing on the applications of MALDI and ESI mass spectrometry.