The development of analytical method for sialylated glycans and glycoproteins by aminolysis-SALSA

2021 Fiscal Year Final Research Report

• Project/Area Number: 19K15597
• Research Category: Grant-in-Aid for Early-Career Scientists
• Allocation Type: Multi-year Fund
• Review Section: Basic Section 34020:Analytical chemistry-related
• Research Institution: Hokkaido University
• Principal Investigator: Hanamatsu Hisatoshi 北海道大学, 医学研究院, 特任助教 (70734185)
• Project Period (FY): 2019-04-01 – 2022-03-31
• Keywords: 糖鎖解析 / シアル酸 / 質量分析 / グライコミクス

Outline of Final Research Achievements

In order to develop novel analytical methods for sialylated glycans and glycoproteins/peptides, we investigated the application of sialic acid linkage-specific alkylamidation via lactone ring-opening aminolysis, termed as aminolysis-SALSA. In this study, we developed comparative and quantitative glycomic analysis by isotope labeling of α2,3-linked sialic acid residues and purification and concentration method of sialylated glycoproteins/peptides using biotin-derivatized amine reagents.Moreover, we found that α2,3 sialyl linkage-specific amidation of esterified sialoglycans can be achieved via an intramolecular lactone, and reported as lactone-driven ester-to-amide derivatization method.

Free Research Field

分析化学

Academic Significance and Societal Importance of the Research Achievements

本研究で開発した、安定同位体試薬を用いた α2,3シアル酸特異的修飾法、ビオチン誘導体化アミン試薬を用いたシアリル化糖タンパク質/ペプチドの修飾法は、疾患糖鎖バイオマーカー探索、投薬による治療効果のモニタリング、血液、細胞、組織など多様な生体サンプルからの α2,3シアル酸を有する糖タンパク質/ペプチド特異的な精製・濃縮などへの応用が期待される。また、エステル-アミド交換法はシアル酸結合様式の識別だけではなく、分岐構造を持つ糖鎖の識別も可能であり、より詳細な糖鎖構造異性体の識別に繋がる。