Abstract. In a study of the metal-related ion generation mechanism in matrix-assisted laser desorption ionization (MALDI), crystals of matrix used in MALDI were grown from matrix-and salt-containing solutions. The intensities of metal ion and metal adducts of the matrix ion obtained from unwashed crystals were higher than those from crystals washed with deionized water, indicating that metal ions and metal adducts of the matrix ions are mainly generated from the surface of crystals. The contributions of preformed metal ions and metal adducts of the matrix ions inside the matrix crystals were minor. Metal adducts of the matrix and analyte ion intensities generated from a mixture of dried matrix, salt, and analyte powders were similar to or higher than those generated from the powder of dried droplet crystals, indicating that the contributions of the preformed metal adducts of the matrix and analyte ions were insignificant. Correlation between metal-related ion intensity fluctuation and protonated ion intensity fluctuation was observed, indicating that the generation mechanism of the metal-related ions is similar to that of the protonated ions. Because the thermally induced proton transfer model effectively describes the generation of the protonated ions, we suggest that metal-related ions are mainly generated from the salt dissolution in the matrix melted by the laser.
In this study, ultraviolet (UV) laser desorption and vacuum UV single-photon (VUV SP) postionization were performed to ionize and successfully analyze 20 common amino acids. The analytical merit and efficiency of the ionization was compared with those of conventional UV matrix-assisted laser desorption ionization (UV-MALDI). A VUV light source (118 nm) was generated from the ninth harmonic of a Q-switched Nd:YAG laser, and the photon number was determined to be larger than 10 12 for each laser pulse in the ionization region. In general, the detection sensitivity of VUV-SP-postionization was 10-100 times higher than that of conventional UV-MALDI. In particular, the ion signal from VUV-SP-postionization was considerably larger than that from UV-MALDI for analytes with low proton affinity such as glycine. However, some fragmentation of intact ions was observed in VUV-SP-postionization. Quantitative analysis performed using a glycine/histidine mixture and tryptophan/phenylalanine mixture revealed that the dynamic range of VUV-SP-postionization was one order of magnitude larger than that of UV-MALDI, indicating that VUV-SP-postionization is suitable for the quantitative analysis of amino acids.
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