Glycosylation of the polypropylene membrane surface via thiol-yne click chemistry for lectin adsorption.

Glycosylated membrane, as one of the most important affinity membranes, permits affinity separation/purification of proteins based on carbohydrate-protein interactions. It is an important scientific issue to screen facile method for fabricating the glycosylated membrane surface with high glycosyl density. Such a surface can be fabricated by the direct covalent immobilization of carbohydrate ligands on the surfaces of microporous polypropylene membrane (MPPM). First, alkyne-functionalized membrane surface was fabricated by plasma pretreatment combined with UV-induced graft polymerization of 3-(trimethylsilyl) propargyl methacrylate. Then, the glycosylated membrane surface was directly fabricated with the thiol-yne click reaction to ensure rapid process, improved efficiency, and high glycosyl density. Chemical and physical properties of the membrane surface were characterized by ATR/FT-IR, XPS, FESEM and water contact angle measurement. Static lectin adsorption indicates that the glycosylated membrane can specifically adsorb lectin concanavalin A (Con A) other than peanut agglutinin (PNA). Break through curves from dynamic Con A adsorption show the membrane has unique properties such as strong specificity, high adsorption capacity, and reversible binding capability. We suggest that the prepared glycosylated membrane is of great potentials in affinity membrane chromatography for rapid and high-resolution separation/purification of lectins.