A constraint scaffold enhances affinity of a bivalent N-acetylglucosamine ligand against wheat germ agglutinin

Revealing biomedically relevant cell and lectin type-dependent structure–activity profiles for glycoclusters by using tissue sections as an assay platform

“…inhibitory potency. 40,41 Besides spatial aspects, the ne-specicities of lectins may well differ. Since more than a dozen folds with diverse molecular architecture and quaternary structure have developed the capacity to act as lectins, "lectins considered 'identical' in terms of monosaccharide specicity possess the ability to recognize ne differences in more complex structures" 42 and protein engineering facilitates custom-made tailoring, this is possible: the group of selected lectins is presented in the next section.…”

Use of a Longer Aglycon Moiety Bearing Sialyl α(2→3) Lactoside on the Glycopolymer for Lectin Evaluation

“…Glycopolymers can be used as sugar-cluster substances [ 5 , 6 ], and various glycopolymers have been used as multivalent-type carbohydrate substrates for determining lectin—carbohydrate interactions [ 7 , 8 ]. Our ongoing synthetic studies using multivalent-type carbohydrate substances such as heterofunctional derivatives [ 9 ], glycodendrimers [ 10 ], and glycopolymers [ 11 ] showed effective enhancement of protein—carbohydrate interaction. Glycopolymers having SLac moieties as epitopes for the carbohydrate chain recognition protein on the mumps virus [ 12 ] were prepared, and they showed inhibitory potency against mumps viruses [ 13 ].…”

Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities

“… 21 In our previous work, the double biotin group provided a divalent sugar ligand linked to it with a favorable orientation for binding to wheat germ agglutinin lectin, resulting in interaction with high binding affinity. 22 Even if the divalent sugar ligand is replaced by other biomolecules, it is expected that their functionality will be well retained. Here, we present new biotinylation reagents 1 and 2 , which have a design with mono and double-biotin functionality directly linking to a pyridazinedione (PD) scaffold ( Figure 1 ).…”

“…If biotin is made divalent, it would form a tight complex by divalent binding to a single avidin molecule rather than monovalent biotin or form oligomers by cross-linking multiple avidin molecules, which are expected to expand applications of avidins . In our previous work, the double biotin group provided a divalent sugar ligand linked to it with a favorable orientation for binding to wheat germ agglutinin lectin, resulting in interaction with high binding affinity . Even if the divalent sugar ligand is replaced by other biomolecules, it is expected that their functionality will be well retained.…”