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Sequencing of glycosaminoglycans with potential to interrogate sequence-specific interactions.


ABSTRACT: Technologies to sequence nucleic acids/proteins are widely available, but straightforward methodologies to sequence complex polysaccharides are lacking. We here put forward a strategy to sequence glycosaminoglycans, long linear polysaccharides involved in many biochemical processes. The method is based on the covalent immobilization and (immuno)chemical characterization of only those size-separated saccharides that harbor the original reducing end of the full-length chain. Using this methodology, the saccharide sequence of the chondroitin sulfate chain of the proteoglycan bikunin was determined. The method can be performed in any standard biochemical lab and opens studies to the interaction of complex saccharide sequences with other biomolecules.

SUBMITTER: van Kuppevelt TH 

PROVIDER: S-EPMC5665995 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Sequencing of glycosaminoglycans with potential to interrogate sequence-specific interactions.

van Kuppevelt Toin H TH   Oosterhof Arie A   Versteeg Elly M M EMM   Podhumljak Emina E   van de Westerlo Els M A EMA   Daamen Willeke F WF  

Scientific reports 20171101 1


Technologies to sequence nucleic acids/proteins are widely available, but straightforward methodologies to sequence complex polysaccharides are lacking. We here put forward a strategy to sequence glycosaminoglycans, long linear polysaccharides involved in many biochemical processes. The method is based on the covalent immobilization and (immuno)chemical characterization of only those size-separated saccharides that harbor the original reducing end of the full-length chain. Using this methodology  ...[more]

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