Peroxidative depolymerization of fucosylated glycosaminoglycan: Bond-cleavage pattern and activities of oligosaccharides

Peroxidative depolymerization is often used to elucidate the structure and structure-activity relationship of fucosylated glycosaminoglycan (FG), while the selectivity of bond cleavage and structural characteristics of the resulting fragments remain to be confirmed. Here, the FG from Stichopus variegatus (SvFG) was depolymerized by H2O2, and a series of yielded mono- and oligo-saccharides were purified. Almost all the non-reducing ends of oligosaccharides were D-GalNAc4S6S, suggesting that GlcA-beta 1,3-GalNAc4S6S linkage was preferentially cleaved. The model reactions showed the glycosidic bond of uronate was more susceptible than those of N-acetyl hexosamine and fucose, which should be due to bond energy of the anomeric C-H. The reducing ends of oligosaccharides include C4-C6 saccharic acid and GalNAc or GalNAcA, which should be derived from the oxidation of the reducing end. A hexasaccharide with tartaric acid exhibited increased anti-iXase activity, suggesting the oxidation of reducing end did not impair the anti-iXase activity of FG-derived oligosaccharides.

Automated summary

Peroxidative depolymerization of fucosylated glycosaminoglycan (FG) from Stichopus variegatus (SvFG) was performed to obtain mono- and oligo-saccharides. The preferential cleavage of GlcA-beta 1,3-GalNAc4S6S linkage and the susceptibility of uronate glycosidic bond were observed. The oxidation of the reducing end did not impair the anti-iXase activity of FG-derived oligosaccharides.