Protein glycosylation is a vital biological process that regulates cellular functions. Scientists at Fudan University developed a glycopeptide enrichment strategy called HG-TCs, allowing the identification of multiple glycosylation types simultaneously. This method can enrich glycopeptides using an azide-alkyne cycloaddition reaction and release them through trypsin cleavage, minimizing sample loss. The approach offers a time-efficient workflow that identified over 900 O-GlcNAc sites and 800 N-glycosites in HeLa cells in a single experiment. The study also revealed distinct spatial glycosylation patterns in HeLa cells under oxidative stress, offering insights into glycosylation’s dynamic roles in cellular responses and disease mechanisms. This research is significant for understanding glycosylation in diseases like cancer.
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New strategy revolutionizes glycoproteomics research
