Chemistry Reference
In-Depth Information
Figure 13.3 A schematic summary of the galectins. (a) Galectins with one carbohydrate-
binding domain and (b) their noncovalent dimers. (c) Galectin-3 has a collagen-like domain
and a carbohydrate-binding domain. (d) Galectins with two covalently linked carbohydrate-
binding domains.
oriented for interaction with the binding site on the lectin (Gestwicki et al. 2002). The
shape of the framework and the length and flexibility of the tether between the frame-
work and the carbohydrate are two critical features of the framework's architecture
that must be considered.
Because the carbohydrate-binding sites on lectins with which the synthetic glyco-
systems are designed to interact may be displayed facing many different directions,
many frameworks have been reported. Flexible linear polymers with appended
sugars, for example, can readily adjust their shape to interact with a variety of
lectins, whereas carbohydrate-functionalized gold nanoparticles should be far more
rigid. Other frameworks that have been reported for the study of protein-
carbohydrate interactions include star polymers, small glycoclusters, carbohydrate-
functionalized viruses, cyclodextrins, pseudopolyrotaxanes,
liposomes, micelles,
vesicles, proteins, surfaces, and dendrimers (Fig. 13.4).
Figure 13.4 A schematic showing some of the frameworks that have been reported for the study
of protein-carbohydrate interactions. Carbohydrates are represented as cyclohexane. (Top)
Glycodendrimer, carbohydrate-functionalized nanoparticle, and star polymer. (Bottom) Linear
glycopolymer, carbohydrate-functionalized protein, and carbohydrate-functionalized surface.
