HOMOGENEOUS GLYCOPEPTIDES AND GLYCOPROTEINS FOR BIOLOGICAL INVESTIGATION

• Published in: Annual review of biochemistry 2002-01, Vol.71 (1), p.593-634
• Main Authors: Grogan, Michael J, Pratt, Matthew R, Marcaurelle, Lisa A, Bertozzi, Carolyn R
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Chemical synthesis; chemoselective ligation; Glycopeptides - chemical synthesis; Glycopeptides - chemistry; Glycopeptides - metabolism; Glycoproteins; Glycoproteins - chemical synthesis; Glycoproteins - chemistry; Glycoproteins - metabolism; Glycosylation; Glycosylphosphatidylinositols - metabolism; GPI anchor; Humans; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mucins - chemistry; N-linked; O-linked; oligosaccharide; P-Selectin - metabolism; Proteins; Serine - chemistry; Threonine - chemistry
• ISSN: 0066-4154; 1545-4509
• DOI: 10.1146/annurev.biochem.71.110601.135334

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.