| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Outline of Final Research Achievements |
Methods for the proteomic analysis have been established using ESI-MS interfaced with liquid chromatography. If all the peptide ion peaks from a protein digest can be detected in a mass spectrum, accurate identification of the protein can be achieved. However, it is difficult to detect the all tryptic digests because of the different ion yields for each peptide fragment. The ion yields of peptides are strongly dependent upon their physicochemical properties. I have studied the effects of the hydrophobic amino acid Phe residue and the influence of its position in peptides on the positive- and negative-ion yields in ESI. Hydrophobic peptides containing Phe residue(s) were potentially advantageous to the vaporization process from the charged droplet to the gas-phase in ESI, resulting in increased total ion yields in both positive- and negative-ion ESI. The enhancement effect of hydrophobicity on the ion yields was higher than that of basicity and acidity of the peptides in ESI.
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