Each sugar-modified (glycosylated) molecule carries hidden information that is regarded as cryptic “sugar code”. Deciphering is accomplished by lectin proteins (e.g. galectins and toxins), which mediate important cellular signals via reversible binding of certain carbohydrate moieties. Proper translation is indispensable for cell homeostasis and changes can have far-reaching consequences.
In nature, the major trigger of adjusting interaction strength between glycosylated compounds and their counterparts (lectins) is multivalency. The higher the density of presented glycans in close proximity the stronger is the lectin binding. So, the approximation of natural surroundings is necessary whenever a protein-glycan interaction is studied in vitro. For these purposes, different scaffolds, namely glycopolymer brushes, neo-glycoproteins and microgels are developed for specifically addressing certain lectins.