AI Article Synopsis
- Proteomics analysis of O-GalNAc glycosylation is vital for finding biomarkers and evaluating how therapies work, but current methods are not very effective.
- The study developed a new enrichment method using Ti-IMAC(IV) materials, which can successfully isolate intact O-GalNAc glycopeptides from tiny amounts of human serum, identifying almost 200 glycopeptides from just 0.1 μL.
- The research yielded the largest O-GalNAc glycosylation database from a small sample size and found 52 glycopeptides that changed significantly in hepatocellular carcinoma patients, emphasizing the method's potential for biomarker discovery.
Article Abstract
Proteomics analysis of O-GalNAc glycosylation is important for the screening of biomarkers and the assessment of therapeutic responses. However, its analysis still faces challenges due to the poor performance of currently available enrichment methods. In this study, an enrichment method was established on the basis of Ti-IMAC(IV) materials, which could enrich the intact O-GalNAc glycopeptides via both the hydrophilic interaction and affinity interaction. This method enabled nearly 200 intact O-GalNAc glycopeptides identified from only 0.1 μL of human serum. This was nearly 2-fold different from that of the HILIC method. An in-depth analysis of the O-GalNAc glycosylation was performed, and 2093 intact glycopeptides were identified from 7.2 μL of human serum samples. This is the largest O-GalNAc glycosylation database of human serum from a trace amount of sample. Furthermore, 52 significantly changed intact O-GalNAc glycopeptides were determined by the quantitative analysis of hepatocellular carcinoma (HCC) and control serum samples, indicating the potential applications of this enrichment method in biomarker discovery.
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