Historical overview of glycoanalysis.
More than half of all human proteins are glycosylated. Glycosylation defines the adhesive properties of glycoconjugates and it is largely through glycan-protein interactions that cell-cell and cell-pathogen contacts occur. Not surprisingly, considering the central role they play in molecular encounters, glycoprotein and carbohydrate-based drugs and therapeutics represent a greater than $20 billion market. Glycomics, the study of glycan expression in biological systems, relies on effective analytical techniques for correlation of glycan structure with function. This overview summarizes techniques developed historically for glycan characterization as well as recent trends. Derivatization methods key to both traditional and modern approaches for glycoanalysis are described. Monosaccharide compositional analysis is fundamental to any effort to understand glycan structure-function relationships. Chromatographic and electrophoretic separations are key parts of any glycoanalytical workflow. Mass spectrometry and nuclear magnetic resonance are complementary instrumental techniques for glycan analysis. Finally, microarrays are emerging as powerful new tools for dynamic analysis of glycan expression.
Bielik
Alicia M
AM
Department of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Zaia
Joseph
J
D000818:Animals; D001671:Biochemistry / Q000266:history / Q000379:methods; D002845:Chromatography / Q000379:methods; D004586:Electrophoresis / Q000379:methods; D054794:Glycomics / Q000266:history* / Q000379:methods; D006031:Glycosylation; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D009005:Monosaccharides / Q000737:chemistry; D011134:Polysaccharides / Q000737:chemistry; D040081:Protein Array Analysis
D009005:Monosaccharides; D011134:Polysaccharides