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Updated: Jul 13, 2026

Rapid Glyco-Qualitative Assessment of Recombinant Proteins Using a Fully Automated System
Published on: June 28, 2024
Self-recognition of N-linked glycans with multivalent GlcNAc, determined as ceramide mimetic conjugate
Seon-Joo Yoon1, Shoko Ikeda, Martin Sadilek
1Division of Biomembrane Research, Pacific Northwest Research Institute, Department of Pathobiology, University of Washington, Seattle, WA 98195, USA.
Abstract:
Aminoceramide mimetic was synthesized and conjugated to N-linked oligosaccharides having multivalent GlcNAc by reductive amination. Ceramide mimetic conjugates with "complex-type" glycan having five or six GlcNAc termini (termed Os Fr. B-Cer) were purified, analyzed by thin-layer chromatography (TLC), and finally characterized by MS/MS analysis through liquid chromatography/mass spectrometry. Binding of Os Fr. B-Cer placed on solid phase polystyrene surface with [3H]cholesterol-labeled liposomes containing Os Fr. B-Cer, or containing various glycosphingolipids (GSLs) was determined. The binding of Os Fr. B-Cer liposomes to Os Fr. B-Cer coated plate was significantly higher than binding of GM3 liposomes. Other GSL liposomes showed no binding. Thus, self-recognition of Os Fr. B-Cer was clearly demonstrated using ceramide mimetic conjugates.
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