Mass Spectrometry
Online ISSN : 2186-5116
Print ISSN : 2187-137X
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Volume 1 , Issue 1
Special Issue: Advanced techniques of MALDI-TOF MS in ionization, instrumentation and applications
Showing 1-8 articles out of 8 articles from the selected issue
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Preface
Editorial
Review
  • Daiki Asakawa, Motoshi Sakakura, Mitsuo Takayama
    Type: Review
    Volume 1 (2012) Issue 1 Pages A0002
    Released: July 05, 2012
    JOURNALS FREE ACCESS
    MALDI-ISD of peptides were studied using several salicylic acid derivatives, 2,5-dihydroxybenzoic acid (2,5-DHB), 5-aminosalicylic acid (5-ASA), 5-formylsalicylic acid (5-FSA), and 5-nitrosalicylic acid (5-NSA) as matrices. The difference in the nature of the functional group at the 5-position in the salicylic acid derivatives can dramatically affect the ISD products. The use of 2,5-DHB and 5-ASA leads to “hydrogen-abundant” peptide radicals and subsequent radical-induced N–Cα bonds cleavage. N–Cα bond cleavage gave a c′/ fragment pair and radical -series fragments gain a hydrogen radical or react with a matrix radical. In contrast, the use of 5-NSA resulted in the production of a “hydrogen-deficient” peptide radical that contained a radical site on the amide nitrogen in the peptide backbone. Subsequently, the radical site on the amide nitrogen induces Cα–C bond dissociation, leading to /x fragment pair. The -series ions undergo further hydrogen abstraction to form a-series ions after Cα–C bond cleavage. Since the Pro residue does not contain a nitrogen-centered radical site, Cα–C bond cleavage does not occur. Alternatively, the specific cleavage of CO–N bonds leads to a /y fragment pair at Xxx–Pro which occurs via hydrogen abstraction from the Cα–H in the Pro residue. The use of 5-FSA generated both /x- and c′/-series fragment pairs. An oxidizing matrix provides useful complementary information in MALDI-ISD compared to a reducing matrix for the analysis of amino acid sequencing and site localization in cases of phosphopeptides. MALDI-ISD, when used in conjunction with both reducing and oxidizing matrices is a potentially useful method for de novo peptide sequencing.
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  • Yousef Gholipour, Rosa Erra-Balsells, Hiroshi Nonami
    Type: Review
    Volume 1 (2012) Issue 1 Pages A0003
    Released: July 05, 2012
    JOURNALS FREE ACCESS
    In this work we describe the use of a combination of a cell pressure probe and a UV-matrix-assisted laser desorption/ ionization time of flight (UV-MALDI-TOF) mass spectrometer for the in situ picoliter sampling and shotgun metabolite profiling of living single cells of plants. In addition to quantifiable sampling, the pressure probe has some unique features which differentiate it from other single-cell analytical tools. Cell wall and plasma membrane properties and water relations of in situ living single cells can be analyzed before sampling the cell sap. In addition, the fully-controlled sampling of cells located at different depths in plant tissues, measurement of the sample volume, and the addition of internal standards are facilitated by the pressure probe. Using a variety of organic compounds and nanoparticles as UV-MALDI matrices, metabolites from neutral carbohydrates to amino acids and other metabolites can be detected through UV-MALDI-TOF mass spectrometry analyses of picoliter-sized, single-cell samples.
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  • Akiko Kubo, Mayumi Kajimura, Makoto Suematsu
    Type: Review
    Volume 1 (2012) Issue 1 Pages A0004
    Released: July 05, 2012
    JOURNALS FREE ACCESS
    Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is capable of determining the distribution of hundreds of molecules at once directly from tissue sections. Since tissues are analyzed intact without homogenization, spatial relationships of molecules are preserved. The technology is, therefore, undoubtedly powerful to investigate the molecular complexity of biological processes. However, several technical refinements are essential for full exploitation of MALDI-IMS to dictate dynamics alteration of biomolecules in situ; these include ways to collect tissues, target-specific tissue pretreatment, matrix choice for effcient ionization, and matrix deposition method to improve imaging resolution. Furthermore, for MALDI-IMS to reach its full potential, quantitative property in the IMS should be strengthened. We review the challenges and new approaches for optimal imaging of proteins, lipids and metabolites, highlighting a novel quantitative IMS of energy metabolites in the recent literature.
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Original Article
  • Mitsuo Takayama, Issei Osaka, Motoshi Sakakura
    Type: Original Article
    Volume 1 (2012) Issue 1 Pages A0001
    Released: June 29, 2012
    JOURNALS FREE ACCESS
    The susceptibility of the N-Cα bond of the peptide backbone to specific cleavage by in-source decay (ISD) in matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) was studied from the standpoint of the secondary structure of three proteins. A naphthalene derivative, 5-amino-1-naphtol (5,1-ANL), was used as the matrix. The resulting c’-ions, which originate from the cleavage at N-Cα bonds in flexible secondary structures such as turn and bend, and are free from intra-molecular hydrogen-bonded α-helix structure, gave relatively intense peaks. Furthermore, ISD spectra of the proteins showed that the N-Cα bonds of specific amino acid residues, namely Gly-Xxx, Xxx-Asp, and Xxx-Asn, were more susceptible to MALDI-ISD than other amino acid residues. This is in agreement with the observation that Gly, Asp and Asn residues usually located in turns, rather than α-helix. The results obtained indicate that protein molecules embedded into the matrix crystal in the MALDI experiments maintain their secondary structures as determined by X-ray crystallography, and that MALDI-ISD has the capability for providing information concerning the secondary structure of protein.
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  • Tohru Yamagaki, Takehiro Watanabe
    Type: Original Article
    Volume 1 (2012) Issue 1 Pages A0005-
    Released: July 20, 2012
    JOURNALS FREE ACCESS
    We studied the ionization process of aromatic carboxylic acids, including ones with or without hydroxy groups in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), because many natural products, metabolites, and drags contain those structural units. In the actual experimental data, benzoic acid was ionized as only deprotonated molecule [M-H]. In contrast, both of negative molecular ion M and deprotonated molecule [M-H] were generated from 2-naphthoic acid and 2-anthracenecarboxylic acid, and the ratio of negative molecular ion to deprotonated molecule M/[M-H] was increased in 2-anthracenecarboxylic acid. In addition, the ratio of 2-anthracenecarboxylic acid was much higher than those of 1- and 9-anthracenecarboxylic acids among the three isomers. Therefore, 2-substitution induced the generation of the negative molecular ion M, which can made us prediction of the substituted positions from their overlapping peak isotope patterns. 2,5-Dihydroxybenzoic acid showed two deprotonated molecules, [M-H] and [M-H*-H], which was generated from a neutral hydrogen radical (H*) removal from a phenolic hydroxy group. The deprotonated molecule [M-H*-H] of 2,5-DHBA was the most abundant among six dihydroxybenzoic acids and three hydroxybenzoic acid. This observation raises the possibility that such a property of 2,5-DHBA could be a clue to explain its highest efficiency as a MALDI matrix. The order of the hydrogen radical removal from the phenolic hydroxy groups was the 3-<4-<<5-positions in the dihydroxybenzoic acids, and the 3-<4-positions in hydroxybenzoic acids. The intra-molecular hydrogen bonding between 1-carboxy and 2-hydroxy groups was an important factor in hydrogen radical removal in the hydroxylbenzoic acids and dihydroxybenzoic acids.
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  • Takashi Nishikaze, Hisako Okumura, Hiroshi Jinmei, Junko Amano
    Type: Original Article
    Volume 1 (2012) Issue 1 Pages A0006-
    Released: August 28, 2012
    JOURNALS FREE ACCESS
    A standard dried-droplet preparation using 2,5-dihydroxybenzoic acid (2,5-DHBA) as the matrix results in a large variation in signal intensity and poor shot-to-shot reproducibility in matrix-assisted laser desorption/ionization (MALDI). We expected that the differences can be attributed to the nature of the crystal structures in the region of the “sweet spot” within the MALDI samples. 2,5-DHBA crystals with and without analytes on a target plate obtained by means of a dried-droplet preparation contain two polymorphs, which can be distinguished by Raman spectra. In comparing the Raman image with the MS image, a clear correlation between the signal distribution of glycopeptides and hydrophilic peptides and the specific crystal form of 2,5-DHBA could be made. The ionization of hydrophobic peptides appears to proceed in both types of polymorphic crystals. In addition, the derivatization of glycopeptides with a pyrene group enabled us to detect glycopeptides regardless the crystal form. As the result, the number of sweet spots increased and MS spectra with a high signal intensity were obtained. The results suggest that the introduction of a hydrophobic/aromatic moiety to glycopeptides results in a more successful MALDI analysis due to the effective incorporation of the analyte into matrix crystals.
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