Formation of glyco-functionalized interfaces for protein binding using polyphenolic glycoside.

Hirokazu Seto, Mao Harada, Hidenori Nagaura, Honoka Taniguchi, Tatsuya Murakami, Ichiro Kimura, Yumiko Hirohashi, Hiroyuki Shinto

Carbohydrate research 2020 Jun

filter terms:

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. Copyright © 2020 Elsevier Ltd. All rights reserved.

Citation

Hirokazu Seto, Mao Harada, Hidenori Nagaura, Honoka Taniguchi, Tatsuya Murakami, Ichiro Kimura, Yumiko Hirohashi, Hiroyuki Shinto. Formation of glyco-functionalized interfaces for protein binding using polyphenolic glycoside. Carbohydrate research. 2020 Jun;492:108002