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Tools to MSn Sequence and Document the Structures of Glycan Epitopes
Hailong Zhang1, David J Ashline2, Vernon N Reinhold3
1The Glycomics Center, University of New Hampshire, Durham, NH 03824, USA.
Discovering the Subtleties of Sugars : Proceedings of the 3Rd Beilstein Glyco-Bioinformatics Symposium : June 10Th - 14Th, 2013, Potsdam, Germany. International Beilstein Symposium on Glyco-Bioinformatics (3Rd : 2013 : Potsdam, Germany)
|April 26, 2016
Summary
This study demonstrates sequential mass spectrometry (MSn) for characterizing native and synthetic glycan epitopes. The method accurately matches native samples with synthetic analogues, confirming structural isomers and linkage patterns.
Area of Science:
- Analytical Chemistry
- Glycobiology
- Mass Spectrometry
Background:
- Characterizing complex carbohydrates like glycan epitopes is crucial in biological research.
- Distinguishing between structural isomers of glycans presents a significant analytical challenge.
Purpose of the Study:
- To develop and validate a sequential mass spectrometry (MSn) approach for the comprehensive characterization of native and synthetic glycan epitopes.
- To compare the fragmentation patterns of native glycans with their synthetic counterparts.
Main Methods:
- Samples were prepared using methylation and solvent phase extraction.
- Direct infusion and spatial resolution were employed for analysis.
- Sequential mass spectrometry (MSn) was utilized to fragment and analyze glycan structures.
- Computational tools were used for data management and presentation.
Main Results:
- Native glycan epitopes were successfully matched with their synthetic analogues.
- MSn analysis confirmed the presence of multiple structural isomers, including variations in linkage and branching.
- Fragmentation patterns were consistent across linear and cylindrical ion traps.
- Spectra of mixed epitopes fragmented independently, unaffected by similarities.
Conclusions:
- Sequential mass spectrometry (MSn) provides a robust method for characterizing glycan epitopes.
- The approach enables accurate differentiation of glycan structural isomers.
- This technique facilitates the comparison of native biological samples with synthetic standards.
