Study on ion yield of phosphorylated peptides in ESI for proteomic analysis

2014 Fiscal Year Final Research Report

• Project/Area Number: 24619006
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: オミクス計測科学
• Research Institution: Japan Advanced Institute of Science and Technology (2013-2014); Yokohama City University (2012)
• Principal Investigator: OSAKA Issey 北陸先端科学技術大学院大学, ナノマテリアルテクノロジーセンター, 講師 (90550244)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: ESI / プロテオミクス / イオン収量 / ペプチド

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.

Free Research Field

質量分析学