An improvement on mass spectrometry-based epigenetic analysis of large histone-derived peptides by using the Ionization Variable Unit interface |
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| Authors: | Tetsuya Fukuda Hiroshi Hike Fumihiko Usui Yasuhiko Bando Toshihide Nishimura Tatsuhiko Kodama Takeshi Kawamura |
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| Institution: | 1. Research and Development, Biosys Technologies, Meguro-Ku, Tokyo 152-0031, Japan;2. AMR, Meguro-Ku, Tokyo 152-0031, Japan;3. Department of Measurement Technology and Electrical Engineering, Division of Clinical Protein Science and Imaging, Center of Excellence in Biological and Medical Mass Spectrometry (CEBMMS), Lund University Biomedical Center, SE-221 84 Lund, Sweden;4. Laboratory for Systems Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo, Meguro-Ku, Tokyo 153-8904, Japan |
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| Abstract: | Highly protonated histone-derived peptides impede a sufficient mass spectrometry (MS)-based epigenetic analysis because their relatively low m/z, due to a high degree of proton addition to peptides, would make it difficult to analyze the resulting complex MS/MS spectra. To reduce the degree of protonations, we have developed a new interface, the Ionization Variable Unit (IVU), in which peptides are ionized under a vaporized organic solvent. It is demonstrated that the doubly charged histone tail H2B peptide, PEPAKSAPAPKKGSKKAVTKAQKK (m/z 1238.243, +2), which was not detectable before, can be detected by using the IVU interface and sequenced. |
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| Keywords: | Charge state conversion Multiply protonated peptides Collision-induced dissociation (CID) Epigenetics Mass spectrometry |
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