Cold-spray ionization mass spectrometry

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  • SEI Yoshihisa
    Chemical Analysis Center, Chiba University CREST, Japan Science and Technology Agency (JST)
  • SHIKII Kazuaki
    Chemical Analysis Center, Chiba University
  • SAKAMOTO Shigeru
    Chemical Analysis Center, Chiba University
  • KUNIMURA Miki
    Chemical Analysis Center, Chiba University
  • KOBAYASHI Tatsuji
    JEOL Ltd.
  • SEKI Hiroko
    Chemical Analysis Center, Chiba University CREST, Japan Science and Technology Agency (JST)
  • TASHIRO Mitsuru
    Department of Chemistry, Faculty of Science, Tokyo Metropolitan University
  • FUJITA Makoto
    Department of Applied Chemistry, School of Enginieering, The University of Tokyo CREST, Japan Science and Technology Agency (JST)
  • YAMAGUCHI Kentaro
    Chemical Analysis Center, Chiba University CREST, Japan Science and Technology Agency (JST)

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Other Title
  • コールドスプレーイオン化質量分析
  • コールドスプレー イオンカ シツリョウ ブンセキ

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Abstract

A direct solution analysis method, cold-spray ionization (CSI) mass spectrometry (MS), a variant of electrospray ionization (ESI) MS operating at low temperature (ca. −80∼15°C ), allows a facile and precise characterization of labile organic species, especially those in which non-covalent bonding interactions are prominent. We have applied this method to investigations of the solution structures of many labile organic species, including unstable reagents and reaction intermediates, asymmetric catalysts, supramolecules, and even primary biomolecules. Remarkable analytical results were obtained for highly ordered supramolecules using the CSI method. While conventional ESI is not applicable to these compounds because of their instability to heat and/or air, CSI affords multiply charged molecular ions with many solvent molecules attached. An investigation of the constitution of Grignard reagents in solution is extremely challenging, but CSI-MS allowed us to identify one of the key structures in a THF solution. Large-scale aggregated chain structures of steroid compounds were observed in diluted solution by means of CSI-MS and PFG NMR. The crystal structures were determined by X-ray crystallography. It is suggested that the intermolecular hydrogen bonding observed in the crystal might be partly retained in diluted solutions. Recently, this method was adopted for investigating of the solution structures of primary biomolecules, such as nucleosides, amino acids, sugars and lipids, revealing singly charged Na+ adducts of large clusters (chain structures), presumably linked by non-covalent interactions, including hydrogen bonding and/or hydrophobic interactions. The principle of the CSI method and applications of the method to a wide variety of labile organic species and biomolecules including protein in solution are described.<br>

Journal

  • BUNSEKI KAGAKU

    BUNSEKI KAGAKU 53 (6), 457-474, 2004

    The Japan Society for Analytical Chemistry

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