Glycosaminoglyclans (GAGs) such as heparin and heparan sulfate are known to influence in vivo activities of several proteins including chemokines. Chemokines are involved in many biological processes such as inflammation and cell development. There is considerable interest in determining the sequence and structure of the GAGs that bind to specific chemokines. We will present a method using affinity capillary electrophoresis (ACE) to study the interaction of heparin-derived oligosaccharides with specific chemokines, such as the stromal cell-derived factor-1 (SDF-1). ACE is well suited for highly anionic analytes such as heparin-derived oligosaccharides, for which large differences in electrophoretic mobility can be observed between the complex and the free target protein. The analytical strategy developed in this study facilitates the identification of heparin-derived oligosaccharide sequences that bind strongly to SDF-1. Knowledge of these interactions can lead to better understanding of how heparin oligosaccharides mediate the biological activities of chemokines.

Studying binding interactions of heparin oligosaccharides with chemokines using affinity capillary electrophoresis

243rd National Meeting (2012)

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