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Published on: November 19, 2018
Formation of glyco-functionalized interfaces for protein binding using polyphenolic glycoside
Hirokazu Seto1, Mao Harada1, Hidenori Nagaura1
1Department of Chemical Engineering, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka, 814-0180, Japan.
Abstract:
In this study, a polyphenolic glycoside (α-glucosyl rutin) was used to form glyco-functionalized interfaces for protein binding. α-Glucosyl rutin was coated onto precious metals, metal oxides, and synthetic polymers, including polyethylene and polytetrafluoroethylene with poor surface modifiability. The glyco-functionalized interfaces bound strongly and specifically to concanavalin A and Bauhinia purpurea lectin, which have different carbohydrate specificities. Competitive adsorption tests demonstrated that the binding sites for the abovementioned lectins were glucosyl and rhamnosyl residues, respectively. The glyco-functionalized interfaces maintained the protein binding ability after being stored in aqueous solution for 1 day and in air for 160 days. Once the glyco-functionalized interfaces were formed on gold, silicon dioxide, polystyrene, and polytetrafluoroethylene using α-glucosyl rutin, all the glyco-functionalized interfaces bound to concanavalin A rather than peanut agglutinin.
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