Identification of Nanomolar Lectin Ligands by a Glycodendrimer Microarray.

ABSTRACT: Carbohydrate-protein interactions play key roles in a wide variety of biological processes. These interactions are usually weak, with dissociation constants in the low millimolar to high micromolar range. Nature uses multivalency to reach high avidities via the glycoside cluster effect. Capitalizing on this effect, numerous synthetic multivalent glycoconjugates have been described and used as ligands for carbohydrate-binding proteins. However, valency is only one of the several parameters governing the binding mechanisms that are different for every biological receptor, making it almost impossible to predict. In this context, ligand optimization requires the screening of a large number of structures with different valencies, rigidities/flexibilities, and architectures. In this article, we

SUBMITTER: Laigre E 

PROVIDER: S-EPMC6210076 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature