{"title":"Advances in mass spectrometry-based strategies for analyzing sialic acid linkage isomers","authors":"Linlin Wu, Mengmeng Wang, Chunfang Gao","doi":"10.1016/j.trac.2025.118383","DOIUrl":null,"url":null,"abstract":"<div><div>Glycosylation is a crucial post-translational modification influencing protein function and disease development. Among glycan structures, α2,3- and α2,6-sialylated glycans exhibit distinct biological roles but are challenging to distinguish due to their structural similarity. Mass spectrometry (MS)-based techniques have become the indispensable platforms for sialic acid linkage isomers characterization, providing unparalleled sensitivity and rapid N-glycans profiling when synergized with complementary analytical strategies. This review focuses on the two main sialic acid linkage isomers, α2,3- and α2,6-, providing a brief overview of their roles in regulating biological functions and emphasizing the urgent need for their accurate detection. The review presents a detailed overview of recent advancements in MS-based methodologies for analyzing sialic acid linkage isomers, including non-derivatization, derivatization, and hybrid approaches. Furthermore, it highlights recent progress in glycomics and glycoproteomics data analysis, proposing theoretical insights to guide the selection of optimal methods for precise isomer identification and quantification.</div></div>","PeriodicalId":439,"journal":{"name":"Trends in Analytical Chemistry","volume":"191 ","pages":"Article 118383"},"PeriodicalIF":12.0000,"publicationDate":"2025-07-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Trends in Analytical Chemistry","FirstCategoryId":"1","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0165993625002511","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, ANALYTICAL","Score":null,"Total":0}
引用次数: 0
Abstract
Glycosylation is a crucial post-translational modification influencing protein function and disease development. Among glycan structures, α2,3- and α2,6-sialylated glycans exhibit distinct biological roles but are challenging to distinguish due to their structural similarity. Mass spectrometry (MS)-based techniques have become the indispensable platforms for sialic acid linkage isomers characterization, providing unparalleled sensitivity and rapid N-glycans profiling when synergized with complementary analytical strategies. This review focuses on the two main sialic acid linkage isomers, α2,3- and α2,6-, providing a brief overview of their roles in regulating biological functions and emphasizing the urgent need for their accurate detection. The review presents a detailed overview of recent advancements in MS-based methodologies for analyzing sialic acid linkage isomers, including non-derivatization, derivatization, and hybrid approaches. Furthermore, it highlights recent progress in glycomics and glycoproteomics data analysis, proposing theoretical insights to guide the selection of optimal methods for precise isomer identification and quantification.
期刊介绍:
TrAC publishes succinct and critical overviews of recent advancements in analytical chemistry, designed to assist analytical chemists and other users of analytical techniques. These reviews offer excellent, up-to-date, and timely coverage of various topics within analytical chemistry. Encompassing areas such as analytical instrumentation, biomedical analysis, biomolecular analysis, biosensors, chemical analysis, chemometrics, clinical chemistry, drug discovery, environmental analysis and monitoring, food analysis, forensic science, laboratory automation, materials science, metabolomics, pesticide-residue analysis, pharmaceutical analysis, proteomics, surface science, and water analysis and monitoring, these critical reviews provide comprehensive insights for practitioners in the field.