Differentiation of 3-O-sulfated heparin disaccharide isomers: identification of structural aspects of the heparin CCL2 binding motif.

Abstract

The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. In this study, tandem mass spectrometry was used to differentiate between two heparin disaccharide isomers containing variable sulfate at C6 in a common disaccharide and C3 in a more rare one. The dissociation patterns shown by MS(2) and MS(3) were clearly distinguishable between the isomers, allowing their differentiation and quantitation. Using this technique, we show that an octasaccharide with 11 sulfate groups with high affinity for inflammatory chemokine CCL2 does not contain 3-O-sulfated disaccharides.

• Authors: John K Meissen, Matthew D Sweeney, Matthew Girardi, Roger Lawrence, Jeffrey D Esko, Julie A Leary
• Journal: Journal of the American Society for Mass Spectrometry (J Am Soc Mass Spectrom) Vol. 20 Issue 4 Pg. 652-7 (Apr 2009) ISSN: 1879-1123 [Electronic] United States
• PMID: 19185514 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)

Chemical References

• Chemokine CCL2
• Disaccharides
• Glycosaminoglycans
• Oligosaccharides
• Sulfates
• heparin disaccharide
• Heparin

Topics

• Animals
• Binding Sites
• CHO Cells
• Chemokine CCL2 (chemistry)
• Cricetinae
• Cricetulus
• Disaccharides (chemistry)
• Glycosaminoglycans (chemistry)
• Heparin (analogs & derivatives, chemistry)
• Humans
• Isomerism
• Oligosaccharides (chemistry)
• Protein Binding
• Sulfates (chemistry)
• Tandem Mass Spectrometry (methods)