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MALDIインソース分解質量分析法による糖タンパク質糖鎖直接解析
Protein glycosylation plays a significant role in many biological processes such as cell-to-cell signaling, recognition, disease, and infection. For example, glycan profile of the cells is significantly changed during cancer, making it a biomarker. Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) is one of the most powerful tools for high-throughput analysis of glycans. In this technique, the choice of matrix affects the ionization efficiency of analyte.
Glycan analysis in glycoproteins require multiple steps; release, separation, modification, etc. The overall procedure is complicated and takes times. In order to minimize the complex processes, we focused on modifying the matrices.
Herein, we demonstrated a novel method for glycomics of intact glycoproteins by MALDI-In-Source Decay (ISD) MS. This method optimized for glycan associated with ISD process gave glycan pattern signal from the intact glycoproteins without any digestion and/or modification processes. The optimization process of the matrix-system focused on aniline derivatives allowed high sensitive and selective ionization of glycan. The glycan ISD products utilizing this novel matrix enabled us to perform pseudo-MS3 strategy to elucidate the structure of each glycan fragments from the glycoproteins.