Year: 2026
Type: article
Abstract: Studies on glycans of glycoproteins are hampered by the lack of standards that reflect the wide diversity in structure typically observed. To this end we have exploited a large library of N -glycan standards comprised of a unique collection of 226 N -glycans including oligomannose, hybrid, and complex-type. We generated a method employing porous graphitized carbon (PGC) and liquid chromatography mass spectrometry (PGC-LC-MS), which can provide a high degree of resolution of underivatized N -glycan structures. Chromatogram libraries arising from these studies include retention time data, diagnostic fragments, and validated structural assignments, providing a robust platform for both targeted and discovery-based glycomics. We refer to this as an N -glycopedia, the first type of resource in which researchers can compare this collective data to N -glycans under study and overcome the limitations of only having compositional data and predicted structures. The technology is easily expandable to include additional N -glycans as new standards become available.
Source: Nature Communications
Authors: Christopher Ashwood, Richard D. Cummings
Institutions: Beth Israel Deaconess Medical Center, Harvard University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,990
Awards: G103575219, Protein-Glycan Interaction Resource at the National Center for Functional Glycomics (NCFG), Engineering Escherichia coli for glycosylation of complex human proteins, G2823094387, G4699841635, G548498090, Humanizing N-linked glycosylation in Escherichia coli, Glycoproteomics and the Glycosylation Code of the Brain in Asymptomatic and Symptomatic Alzheimer’s Disease, G7059131728, A Comprehensive 5K plus Glycan Microarray, G8883367568
OpenAlex ID: W7161807176