Carbohydrate-protein binding interactions

Table 4 Quantitative Methods for Characterization of Carbohydrate-Protein Binding Interactions... 

We and others have previously demonstrated that multivalent neoglycoconju-gates constitute powerful inhibitors in a number of generally low-affinity carbohydrate-protein binding interactions [11-16]. Potent multivalent neoglycoconjugates... 

Neoglycoproteins, liposomes, and glycopolymers have been successfully used to demonstrate that multivalency does indeed amplify carbohydrate-protein binding interactions by factors as high as thousands. However, by their very nature, these neoglycoconjugates have ill-defined chemical structures. They are heterogeneous in size and carbohydrate contents. Additionally, neoglycoproteins have been shown to... 

To explore the concept of using terminal carbohydrate moieties as crucial elements, Hindsgaul et al. [36] developed a new class of compounds — glycohybrids. These compounds represent a unique combination of glycoside moieties combined with amino acids and do not occur in natural systems. Cognizant with the typical weak carbohydrate-protein bindings, the idea was to assist carbohydrate-based weak interactions by additional amino acids that may provide the extra contact points for specific bindings. 

Once multivalent carbohydrate-protein interactions are firmly established with the assistance of neoglycoconjugates such as those described above, further focus toward fine-tuned geometry and valency requirements becomes necessary for a thorough understanding of the binding interactions involved. Until now, these investigations have been more or less dependent on trial and error which... 

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