Sugars are known in binding with proteins specifically, and the sugar-protein intearaction plays important role in biological systems. For example, it is related to virus infection, metastasis of cancer, and cell adherence. However, the interaction of monovalent sugar against protein is weak. Hence, on cell surfaces, sugars exist as clustered domains such as glycolipids and glycoproteins to enhance their interaction against proteins. This cluster effect can be brought out by the synthesis of glycopolymers. Our group recently reported the synthesis of glycopolymers by click chemistry and reversible addition fragmentation chain transfer (RAFT) polymerization. With this method, glycopolymers with different sugar units can be easily synthesized compared to the previous method which glycopolymers are synthesized by the polymerization of pre-synthesized sugar monomers. However, analysis of glycopolymer-protein interaction individually is difficult since there are many kinds of glycans that are related to important biological phenomena. Therefore, preparation of glycopolymer array and exhausitve analysis method is required. In this research, we use surface plasmon resonance imaging (SRPI) method for analyzing interaction between glycopolymers and proteins (Fig. 1). The glycopolymer array was easily prepared by attachment of thiol-terminated glycopolymers synthesized by click chemistry and RAFT polymerization onto SPRI gold chip. The adsorption of proteins onto glycopolymer surfaces were monitored by measuring the reflectivity change of the irradiated light, and the binding process images were taken. The interaction between proteins and various glycopolymers were analyzed. We expect that the results contribute to the development of biomaterials using glycopolymers.

Screening of protein interaction against glycopolymer synthesized by click chemistry

254th National Meeting (2017)

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