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Solving Promiscuous Protein Carbohydrate Recognition Domains with Multivalent Glycofullerenes

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Studies on multivalent carbohydrate protein interactions critically depend on the nature of protein's binding sites, their number and also their relative three dimensional orientations. Although a wide range of neoglycoconjugates including glycodendrimers has been synthesized to address this issue, no systematic rules exist yet that can predict the optimal shapes, size, and number of required exposed carbohydrate ligands. This chapter will illustrate a few examples of bacterial and human lectins together with bacterial toxins having varied number of carbohydrate recognition domains that necessitated multivalent glycoconjugates. In particular, fullerenes, because of their particular physical properties, have been used to describe novel synthetic strategies and possible fit with concomitant lectins.
Title: Solving Promiscuous Protein Carbohydrate Recognition Domains with Multivalent Glycofullerenes
Description:
Studies on multivalent carbohydrate protein interactions critically depend on the nature of protein's binding sites, their number and also their relative three dimensional orientations.
Although a wide range of neoglycoconjugates including glycodendrimers has been synthesized to address this issue, no systematic rules exist yet that can predict the optimal shapes, size, and number of required exposed carbohydrate ligands.
This chapter will illustrate a few examples of bacterial and human lectins together with bacterial toxins having varied number of carbohydrate recognition domains that necessitated multivalent glycoconjugates.
In particular, fullerenes, because of their particular physical properties, have been used to describe novel synthetic strategies and possible fit with concomitant lectins.

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