Glycosaminoglycans (GAGs), such as heparin and heparan sulfates, are known to influence in-vivo activities of a wide range of proteins. GAGs consist of repeat disaccharide units that differ in basic monosaccharide sequence, substitution pattern, and stereochemistry of the glycosidic linkages. The structural complexity of GAG chains present considerable challenges in studying their molecular interactions with proteins. We present an affinity capillary electrophoresis (ACE) method to study GAG-protein interactions. 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. Binding parameters can be obtained reproducibly with minimal sample consumption. Results obtained will be validated using computational approaches and nuclear magnetic resonance (NMR) spectroscopy. Elucidation of GAG-protein interactions can provide critical insight into mechanisms underlying important biological processes.

Affinity capillary electrophoresis for the study of  glycosaminoglycan-protein interactions

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.