Structure elucidation of microgram quantities of heparin oligosaccharides important for protein binding

AEI 6

Albert K. Korir1, John F. K. Limtiaco, limtiacojohn@hotmail.com2, and Cynthia K. Larive, clarive@ucr.edu1. (1) Department of Chemistry, University of California, Riverside, Riverside, CA 92521, (2) Department of Chemistry, University of California Riverside, Riverside, CA 92521
Heparin and the related glycosaminoglycan (GAG) heparan sulfate are highly negatively charged micro-heterogeneous linear polysaccharides that are important participants in many biological processes. While GAGs are known to interact with hundreds of different proteins, the key to understanding these interactions lies in the identification of the heparin motifs important for binding. A major limitation of current studies of GAG structure and function is the time and effort required to isolate sufficient quantities of oligosaccharides for chemical analysis. We are developing a strategy using CE, MS, capillary isotachophoresis – NMR (cITP-NMR) and the use of a commercial Protasis/MRM microcoil NMR probe to analyze enzymatic digests of heparin. This strategy permits the efficient identification of oligosaccharides of interest and their complete structure determination by MS and 2D NMR analysis using only microgram quantities of isolated material, expediting the discovery and structure elucidation of heparin motifs important for binding.
 

Academic Employment Initiative
8:00 PM-10:00 PM, Monday, August 20, 2007 BCEC -- Exhibit Hall - B2, Sci-Mix

Academic Employment Initiative

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007