Comprehensive structural assignment of glycosaminoglycan oligo- and polysaccharides by protein nanopore - Faculté des Sciences de Sorbonne Université Access content directly
Journal Articles Nature Communications Year : 2022

Comprehensive structural assignment of glycosaminoglycan oligo- and polysaccharides by protein nanopore

Abstract

Abstract Glycosaminoglycans are highly anionic functional polysaccharides with information content in their structure that plays a major role in the communication between the cell and the extracellular environment. The study presented here reports the label-free detection and analysis of glycosaminoglycan molecules at the single molecule level using sensing by biological nanopore, thus addressing the need to decipher structural information in oligo- and polysaccharide sequences, which remains a major challenge for glycoscience. We demonstrate that a wild-type aerolysin nanopore can detect and characterize glycosaminoglycan oligosaccharides with various sulfate patterns, osidic bonds and epimers of uronic acid residues. Size discrimination of tetra- to icosasaccharides from heparin, chondroitin sulfate and dermatan sulfate was investigated and we show that different contents and distributions of sulfate groups can be detected. Remarkably, differences in α/β anomerization and 1,4/1,3 osidic linkages can also be detected in heparosan and hyaluronic acid, as well as the subtle difference between the glucuronic/iduronic epimers in chondroitin and dermatan sulfate. Although, at this stage, discrimination of each of the constituent units of GAGs is not yet achieved at the single-molecule level, the resolution reached in this study is an essential step toward this ultimate goal.
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Dates and versions

hal-03782343 , version 1 (28-11-2023)
hal-03782343 , version 2 (21-12-2023)

Identifiers

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Parisa Bayat, Charlotte Rambaud, Bernard Priem, Matthieu Bourderioux, Mélanie Bilong, et al.. Comprehensive structural assignment of glycosaminoglycan oligo- and polysaccharides by protein nanopore. Nature Communications, 2022, 13 (1), pp.5113. ⟨10.1038/s41467-022-32800-4⟩. ⟨hal-03782343v1⟩
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