TY - JOUR
T1 - Glycopolymer monoliths for affinity bioseparation of proteins in a continuous-flow system
T2 - glycomonoliths
AU - Seto, Hirokazu
AU - Shibuya, Makoto
AU - Matsumoto, Hikaru
AU - Hoshino, Yu
AU - Miura, Yoshiko
N1 - Funding Information:
This work was supported by a Grant-in-Aid for JSPS Fellows (25.5206), a Grant-in-Aid for Scientific Research (B) (15H03818), a Grant-in-Aid for Challenging Exploratory Research (16K14007), and Grant-in-Aid for Scientific Research on Innovative Areas (16H01036). The support from Murata Manufacturing Co., Ltd and Izumi Science and Technology Foundation was greatly appreciated. We appreciated assistance from Prof. M. Kamihira, Assoc. Prof. A. Ito, and Assist. Prof. Y. Kawabe at Kyushu University with electrophoresis.
Publisher Copyright:
© The Royal Society of Chemistry.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017
Y1 - 2017
N2 - In this study, macroporous materials, called glycomonoliths, were produced from saccharide-containing monomers, and used for affinity bioseparation of proteins in a continuous-flow system. The porous structure formation of the glycomonoliths involved polymerization-induced phase separation of the polyacrylamide unit. The pore size could be controlled between several hundred nanometers and several micrometers by changing the alcohol used as the porogenic solvent during the preparation of the monolith. The glycomonolith pores allowed for the permeation of solutions through the monoliths, which meant that they could be used in a continuous-flow system. The adsorption capacities of the glycomonoliths for the saccharide-binding protein (concanavalin A) were larger than that of a glycopolymer-grafted material because of the higher saccharide densities in the monoliths than the grafted material. When concanavalin A was eluted from the glycomonolith, the concentration of concanavalin A in the effluent was up to 11 times higher than that in the feed solution. The adsorption of concanavalin A to the glycomonolith was specific, even in the presence of other proteins.
AB - In this study, macroporous materials, called glycomonoliths, were produced from saccharide-containing monomers, and used for affinity bioseparation of proteins in a continuous-flow system. The porous structure formation of the glycomonoliths involved polymerization-induced phase separation of the polyacrylamide unit. The pore size could be controlled between several hundred nanometers and several micrometers by changing the alcohol used as the porogenic solvent during the preparation of the monolith. The glycomonolith pores allowed for the permeation of solutions through the monoliths, which meant that they could be used in a continuous-flow system. The adsorption capacities of the glycomonoliths for the saccharide-binding protein (concanavalin A) were larger than that of a glycopolymer-grafted material because of the higher saccharide densities in the monoliths than the grafted material. When concanavalin A was eluted from the glycomonolith, the concentration of concanavalin A in the effluent was up to 11 times higher than that in the feed solution. The adsorption of concanavalin A to the glycomonolith was specific, even in the presence of other proteins.
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U2 - 10.1039/c6tb02930b
DO - 10.1039/c6tb02930b
M3 - Article
C2 - 32263584
AN - SCOPUS:85012036932
SN - 2050-7518
VL - 5
SP - 1148
EP - 1154
JO - Journal of Materials Chemistry B
JF - Journal of Materials Chemistry B
IS - 6
ER -