Homogeneous Glycopeptides and Glycoproteins for Biological Investigation

Michael J. Grogan(Howard Hughes Medical Institute), Matthew R. Pratt(Howard Hughes Medical Institute), Lisa A. Marcaurelle(Howard Hughes Medical Institute), Carolyn R. Bertozzi(Howard Hughes Medical Institute)
Annual Review of Biochemistry
June 1, 2002
Cited by 162

Abstract

Protein glycosylation is widely recognized as a modulator of protein structure, localization, and cell-cell recognition in multicellular systems. Glycoproteins are typically expressed as mixtures of glycoforms, their oligosaccharides being generated by a template-independent biosynthetic process. Investigation of their function has been greatly assisted by sources of homogeneous material. This review summarizes current efforts to obtain homogeneous glycopeptide and glycoprotein materials by a variety of methods that draw from the techniques of recombinant expression, chemical synthesis, enzymatic transformation, and chemoselective ligation. Some of these techniques remove obstacles to glycoprotein synthesis by installing nonnative linkages and other modifications for facilitated assembly. The end purpose of the described approaches is the production of glycosylated materials for experiments relevant to the biological investigation of glycoproteins, although the strategies presented apply to other posttranslational modifications as well.


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