This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: A research team has developed a reliable, economical laboratory method that uses tiny magnetic beads to study proteins with sugar molecules attached to them in blood and tissue samples. A better understanding of their pathological changes could help researchers diagnose and treat diseases, including cancer.
Their work was published in the journal Molecular & Cellular Proteomics on Aug. 11, 2026. Scientists in Japan started the Human Glycome Atlas (HGA) Project in April 2023 to create a catalog of human sugar molecules, called glycans, related to disease. The catalog is being created using glycoproteomics on a large cohort of samples.
In glycoproteomics, scientists study proteins, called glycoproteins, that have sugar molecules attached to them. Glycoproteomics is a branch of proteomics, the large-scale study of all proteins' function and structure in an organism, tissue or cell. For the HGA Project to achieve its goals, researchers needed to develop faster, more efficient sample-preparation methods that increased analytical throughput.
A research team from Japan has developed a robust method using low-cost, commercially available magnetic particles. Glycosylation, the process of attaching a sugar molecule to a protein or lipid, is the most common chemical change to a protein after it has been built by a cell. How the sugar molecule attaches to the protein affects the protein's interactions with other cells.
Scientists have noted changes in the glycosylation patterns of proteins in several diseases, including cancer. Cancer can alter sugar molecules. These altered sugar proteins are important biomarkers because scientists can find and track cancer by studying changes in the sugar molecules.
Bottom-up glycoproteomics is a promising approach for biomarker discovery because it provides scientists with qualitative and quantitative information on carrier glycoproteins, glycosylation sites and glycan composition. In bottom-up glycoproteomics, scientists use enzymes to cut proteins with attached sugar molecules into smaller pieces called peptides, purify them using a laboratory technique called hydrophilic interaction liquid chromatography (HILIC), and study them using mass spectrometry. However, bottom-up glycoproteomics has limited usefulness because mass spectrometry cannot easily detect glycopeptides when plain proteins are so plentiful.
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