Synthesis of Artificial N-Glycopolypeptides Carrying N-Acetyllactosamine and Related Compounds and Their Specific Interactions with Lectins

Abstract

Artificial N-glycopolypeptides carrying N-acetyllactosamine (LacNAc) or related compounds were synthesized. First, sugars were converted into their corresponding β-glycosylamines with ammonium hydrogen carbonate. Then, the β-glycosylamines were condensated with the carboxyl groups of poly(L-glutamic acid). N-Glycopolypeptides with different degrees of substitution of sugars were isolated by passage through a column of Sephadex G-25. These synthetic polymers were used as model compounds in the analysis of oligosaccharide-lectin interactions. Interactions with some lectins were investigated by agar-gel double-diffusion tests and in terms of inhibition of hemagglutination. A glycopolypeptide substituted with LacNAc reacted with Erythrina cristagalli agglutinin (ECA), peanut (Arachis hypogaea) agglutinin (PNA), Ricinus communis agglutinin-120 (RCA₁₂₀), wheat germ (Triticum vulgaris) agglutinin (WGA) lectins, which recognize either galactosyl or N-acetylglucosamine (GlcNAc) residues. Other synthetic glycopolymers carrying N-acetylisolactosamine, GlcNAc, N,N′-diacetylchitobiose, or N,N′,N″-triacetylchitotriose also reacted with WGA, and these last two polymers inhibited hemagglutination most. Of these five glycopolypeptides, only the one substituted with LacNAc reacted with ECA. These sugar-substituted glycopolypeptides interacted specifically with the corresponding lectins, no matter how much shorter the sugar side chains of the glycopolymers were than those of natural glycoproteins.

• N-glycopolypeptide
• glycopolymer
• lectin
• molecular recognition
• glycotechnology