|Recent Developments in Protein Glycosylation Analysis by HPLC with Charged Aerosol and Mass Spectrometric Detection|
Event Date: Tuesday September 17, 2013 at 8:00 am PDT/ 11:00 am EDT/ 16:00 BST/ 17:00 CEDT
An estimated half of all proteins include carbohydrate moieties that are added during post-translational modification. Glycosylation imparts a staggering degree of molecular diversity and influences protein structure and function. Scientists are currently investigating the role that glycosylation plays in such wide-ranging phenomena as protein folding, stability, clearance, recognition, and cell-cell adhesion. Over 40 disorders of glycosylation have been reported in humans.
It is believed that glycoproteins of biological, diagnostic, or therapeutic interest owe key aspects of their normal function to the oligosaccharides attached to the protein backbone. Variations in the number, type, composition, or linkage pattern of these glycans may influence the efficacy of a bio-therapeutic product. The ability to correctly identify and measure glycans is of scientific interest, and to do so reliably, quickly and inexpensively is of practical benefit.
This web seminar will discuss promising improvements to glycosylation analysis that couple unique HPLC stationary phases with direct measurement of glycans by charged aerosol detection and with flow-splitting for simultaneous mass spectrometry MS-MS detection. These strategies avoid problematic O-linked glycan degradation (“peeling”) associated with some other quantitative methods, and employs optimal conditions for heightened characterization using additional offline MS techniques for characterization.
LCGC North America
Andy Hanneman Ph.D
Glycan Connections, LLC
Dave Thomas Ph.D
Product Applications Scientist
Chromatography and Mass Spectrometry Division
Thermo Fisher Scientific
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