Abstract
Protein–carbohydrate interactions exhibit myriad intracellular recognition events, so understanding and investigating their specific interaction with high selectivity and strength are of crucial importance. In order to examine the effect of multivalent binding on the specificity of protein–carbohydrate interactions, we synthesized mannose glycosides as a novel type of glycosylated monomer and glycopolymers of polyacrylamide derivatives with α-mannose (α-Man) by radical polymerization and monitored their strength of interaction with concanavalin A (Con A) by surface plasmon resonance (SPR) detection. In a quantitative test using the Con A-immobilized sensor surface, the kinetic affinity for the synthesized polymers, 8a (KD = 3.3 × 10−6 M) and 8b (KD = 5.3 × 10−5 M), were concentration-dependent, showing strong, specific molecular recognition abilities with lectin. Our study showed the enhancement in recognition specificity for multivalent saccharides, which is often mediated by cell surface carbohydrate-binding proteins that exhibit weak affinity and broad specificity for the individual ligands.
Highlights
Saccharides on cell surfaces are amongst the most complex and prevalent biomolecules that serve a host of biological functions, including physiological as well as pathological functions in the cell via protein–saccharide interactions that facilitate fundamental cell–cell recognition events in processes such as fertilization, development, and the mounting of an immune response [1,2]
In this study, we report the successful synthesis of mannose glycosides as a novel type of glycosylated monomers and its polymer and investigated the binding selectivity of the synthesized substrate with mannose/glucose-binding protein concanavalin A (Con A)
D -(+)-Mannose was selected as the scaffold for the synthesis of the C-1 modified glycopolymer because of its availability and convenient handling
Summary
Saccharides on cell surfaces are amongst the most complex and prevalent biomolecules that serve a host of biological functions, including physiological as well as pathological functions in the cell via protein–saccharide interactions that facilitate fundamental cell–cell recognition events in processes such as fertilization, development, and the mounting of an immune response [1,2]. The binding of a synthesized glycopolymer to biosensor-immobilized Con A was examined, and this allowed us to determine both the kinetics parameters and affinity constant Ka of the interaction, which may further aid in understanding the biological specificity and functions of both the glycoconjugate and the lectin. We anticipate that this synthetic scaffold will offer new means to define the structures of multivalent ligands and densities of binding epitope for specific functions in the lectin–glycan interactions
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