Glycopolymers are synthetic functional polymers containing numerous saccharide moieties in their side chains. They exhibit the “glycocluster effect,” which is a multivalent effect with glycoreceptors, such as lectins. Recently, there have been several reports on the conjugation of glycopolymers with proteins and antibodies to enhance their functionality. This review summarizes precise methods for synthesizing glycopolymers, their conjugation with proteins, and various applications of glycopolymer-modified proteins. In addition, glycopolymer-modified antibodies, which have received considerable attention in recent years, are discussed.

Glycosylation is one of the most abundant post-translational modifications and is essential for various biological phenomena. Herein, we describe the isolation, structural determination, and chemical synthesis of the N-glycan from the hyperthermophilic archaeon Thermococcus kodakarensis. The N-glycan from the organism possesses a unique structure including myo-inositol, which has not been found in previously characterized N-glycans. In this structure, myo-inositol is highly glycosylated and linked with a disaccharide unit through a phosphodiester. The straightforward synthesis of this glycan was accomplished through diastereoselective phosphorylation and phosphodiester construction by S_N2 coupling. As hyperthermophilic lineages diverged early during evolution, this study can be expected to open the door to approaching the primitive function of glycan modification at the molecular level.

Glycopolymers are synthetic functional polymers containing numerous saccharide moieties in their side chains. They exhibit the “glycocluster effect,” which is a multivalent effect with glycoreceptors, such as lectins. Recently, there have been several reports on the conjugation of glycopolymers with proteins and antibodies to enhance their functionality. This review summarizes precise methods for synthesizing glycopolymers, their conjugation with proteins, and various applications of glycopolymer-modified proteins. In addition, glycopolymer-modified antibodies, which have received considerable attention in recent years, are discussed.

Glycosylation is one of the most abundant post-translational modifications and is essential for various biological phenomena. Herein, we describe the isolation, structural determination, and chemical synthesis of the N-glycan from the hyperthermophilic archaeon Thermococcus kodakarensis. The N-glycan from the organism possesses a unique structure including myo-inositol, which has not been found in previously characterized N-glycans. In this structure, myo-inositol is highly glycosylated and linked with a disaccharide unit through a phosphodiester. The straightforward synthesis of this glycan was accomplished through diastereoselective phosphorylation and phosphodiester construction by S_N2 coupling. As hyperthermophilic lineages diverged early during evolution, this study can be expected to open the door to approaching the primitive function of glycan modification at the molecular level.