Unprecedented Affinity Labeling of Carbohydrate-Binding Proteins with -Triazinyl Glycosides.

Carbohydrate-protein interactions trigger a wide range of biological signaling pathways, the mainstays of physiological and pathological processes. However, there are an incredible number of carbohydrate-binding proteins (CBPs) that remain to be identified and characterized. This study reports for the first time the covalent labeling of CBPs by triazinyl glycosides, a new and promising class of affinity-based glycoprobes.

Efficient Conjugation of Oligosaccharides to Polymer Particles through Furan/Maleimide Diels-Alder Reaction: Application to the Capture of Carbohydrate-Binding Proteins.

Glycan-protein interactions play a crucial role in physiological and pathological events. Hence, improving the isolation of carbohydrate-binding proteins (i.e.

Redox tunable delivery systems: sweet block copolymer micelles via thiol-(bromo)maleimide conjugation.

Oligosaccharide-based block copolymers (OBCPs) are synthesized by thiol click conjugation using reducing-end thiol-containing xyloglucooligosaccharides and maleimide- or bromomaleimide-terminated polycaprolactone. The self-assembled OBCPs in aqueous solution lead to redox-sensitive micelles with different responsiveness. This distinguishing feature allows us to control the release of entrapped hydrophobic Nile red by mixing both OBCPs.