Mass spectrometric characterization of phosphorylated peptides using MALDI in-source decay via redox reactions |
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Authors: | Asakawa Daiki Takayama Mitsuo |
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Affiliation: | Graduate School of Nanobioscience, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan. |
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Abstract: | Matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) has been used for characterization of a phosphorylated peptides and proteins because labile phosphate group is not lost during the MALDI-ISD process. The conventional MALDI-ISD is initiated by the hydrogen transfer from reducing matrix molecules to peptide backbone, leading to c'- and z'-series ions. In contrast, when an oxidizing chemical 5-nitrosalicylic acid (5-NSA) is served as the MALDI-ISD matrix, a- and x-series ions are specifically generated by hydrogen abstraction from peptide backbone to matrix molecule. The 5-NSA provides useful complementary information to the conventional MALDI-ISD for the analysis of amino acid sequencing and site localization of phosphorylation in peptides. The MALDI-ISD with reducing and oxidizing matrix could be a useful method for the de novo peptide sequencing. |
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