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基于质谱的N-糖蛋白分析进展

田志新

田志新. 基于质谱的N-糖蛋白分析进展[J]. 中国药科大学学报, 2023, 54(6): 662-673. DOI: 10.11665/j.issn.1000-5048.2023062701
引用本文: 田志新. 基于质谱的N-糖蛋白分析进展[J]. 中国药科大学学报, 2023, 54(6): 662-673. DOI: 10.11665/j.issn.1000-5048.2023062701
shu
TIAN Zhixin. Progresses of mass spectrometry-based analysis of N-glycoproteins[J]. Journal of China Pharmaceutical University, 2023, 54(6): 662-673. DOI: 10.11665/j.issn.1000-5048.2023062701
Citation: TIAN Zhixin. Progresses of mass spectrometry-based analysis of N-glycoproteins[J]. Journal of China Pharmaceutical University, 2023, 54(6): 662-673. DOI: 10.11665/j.issn.1000-5048.2023062701
shu

基于质谱的N-糖蛋白分析进展

  • 同济大学化学科学与工程学院，上海 200092

基金项目: 国家自然科学基金资助项目（No.22074105，No.21775110，No.21575104）

Progresses of mass spectrometry-based analysis of N-glycoproteins

  • School of Chemical Science and Engineering, TongJi University, Shanghai 200092, China

Funds: This study was supported by the National Natural Science Foundation of China (No.22074105, No.21775110, No.21575104)

摘要

    摘要
  • 摘要: N-连接糖基化是蛋白质上常见的翻译后修饰，在修饰位点上具有跟其他小分子修饰（如甲基化、乙酰化、磷酸化）同样的宏观不均一性，也就是蛋白质氨基酸序列上具有多个潜在的修饰位点。但相对于小分子修饰单一的结构，N-糖基化修饰具有来自不同单糖组成，序列结构、链接结构、异头异构，立体构象等多个结构维度的数以万计的结构。这使得N-糖基化在修饰位点上具有额外的微观不均一性，也就是说同一个N-糖基化位点可以以一定的化学计量比修饰不同的糖链。N-糖基化修饰以位点和结构特异的方式调控N-糖蛋白的结构和功能，疾病条件下差异表达的N-糖基化需通过位点和结构特异的定量分析来表征。本文主要介绍最新发展水平的基于质谱的位点和结构特异定量N-糖蛋白质组学及在生物医学中的应用。
    Abstract: N-linked glycosylation is a common post-translational modification on proteins, which exhibits the same macro-heterogeneity of modification site as other small molecule modifications (such as methylation, acetylation, phosphorylation), i.e., the amino acid sequence of a protein has multiple putative modification sites. However, compared to small molecule modifications with single structures, N-glycosylation modification have tens of thousands of structures from multiple structural dimensions such as different monosaccharide compositions, sequence structures, linking structures, isomerism, and three-dimensional conformation.This results in additional micro-heterogeneity of modification site of N-glycosylation, i.e., the same N-glycosylation site can be modified with different glycans with a certain stoichiometric ratio.N-glycosylation modification regulates the structure and function of N-glycoproteins in a site- and structure-specific manner, and differential expression of N-glycosylation under disease conditions needs to be characterized through site- and structure-specific quantitative analysis.This article mainly introduces the latest development of mass spectrometry-based site- and structure-specific quantitative N-glycoproteomics and its applications in biomedical fields.
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出版历程
  • 收稿日期:  2023-06-26
  • 修回日期:  2023-12-10
  • 刊出日期:  2023-12-24

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