TY - JOUR
T1 - Resistance of surface-confined telomers with pendent glucosylurea groups against non-specific adsorption of proteins
AU - Kitano, Hiromi
AU - Gemmei-Ide, Makoto
AU - Anraku, Yasutaka
AU - Saruwatari, Yoshiyuki
N1 - Funding Information:
This work was supported by a Grant-in-Aid (16205015 and 17750105) from the Japan Society for the Promotion of Science. The authors are grateful to Osaka Organic Chemical Industries, Ltd., for the continuous generous support to pursue this work. The authors are indebted to Messieurs A. Ohtsuki, A. Kawasaki, H. Kawasaki, H. Nakada and K. Matsuura of this laboratory for their technical assistances.
PY - 2007/4/15
Y1 - 2007/4/15
N2 - A disulfide-carrying random telomer with pendent d-glucosylurea groups (Cys-poly(glucosylureaethyl methacrylate-r-ureaethyl methacrylate), Cys-Poly(GUMA-r-UMA)) was obtained by UV-irradiation of GUMA and UMA in the presence of benzyl N,N-diethyldithiocarbamoyl (BDC) derivative which shows the abilities of initiation, transfer, and termination (iniferter). The disulfide-carrying telomer was accumulated on a gold electrode and colloidal gold-immobilized glass substrate, and the binding of various proteins to the surface of the polymer brush was examined by both cyclic voltammetry (CV) with hydroquinone as a probe, and localized surface plasmon resonance (LSPR) absorption method. The Cys-Poly(GUMA-r-UMA) brush did not show a significant non-specific adsorption of proteins such as bovine serum albumin and egg white lysozyme. Furthermore, sugar binding proteins, concanavalin A (with an affinity for mannose and glucose) and wheat germ agglutinin (with an affinity for N-acetylglucosamine), were only slightly adsorbed to the GUMA-carrying brush, which is in contrast with the prompt and distinct binding of these proteins to the brushes composed of 2-methacryloyloxyethyl d-glucopyranoside and 1-(6′-methacrylamido)hexyl-2-N-acetoamido-2-deoxy-d-glucopyranoside, respectively. The glucosylurea group-carrying telomer brush prepared here might be useful to provide a "bio-inert" surface in bio-medical fields.
AB - A disulfide-carrying random telomer with pendent d-glucosylurea groups (Cys-poly(glucosylureaethyl methacrylate-r-ureaethyl methacrylate), Cys-Poly(GUMA-r-UMA)) was obtained by UV-irradiation of GUMA and UMA in the presence of benzyl N,N-diethyldithiocarbamoyl (BDC) derivative which shows the abilities of initiation, transfer, and termination (iniferter). The disulfide-carrying telomer was accumulated on a gold electrode and colloidal gold-immobilized glass substrate, and the binding of various proteins to the surface of the polymer brush was examined by both cyclic voltammetry (CV) with hydroquinone as a probe, and localized surface plasmon resonance (LSPR) absorption method. The Cys-Poly(GUMA-r-UMA) brush did not show a significant non-specific adsorption of proteins such as bovine serum albumin and egg white lysozyme. Furthermore, sugar binding proteins, concanavalin A (with an affinity for mannose and glucose) and wheat germ agglutinin (with an affinity for N-acetylglucosamine), were only slightly adsorbed to the GUMA-carrying brush, which is in contrast with the prompt and distinct binding of these proteins to the brushes composed of 2-methacryloyloxyethyl d-glucopyranoside and 1-(6′-methacrylamido)hexyl-2-N-acetoamido-2-deoxy-d-glucopyranoside, respectively. The glucosylurea group-carrying telomer brush prepared here might be useful to provide a "bio-inert" surface in bio-medical fields.
KW - Adsorption
KW - Cyclic voltammetry
KW - Glucosylurea polymer
KW - Localized surface plasmon resonance
KW - Protein
KW - Telomer brush
UR - http://www.scopus.com/inward/record.url?scp=33947500831&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2006.07.020
DO - 10.1016/j.colsurfb.2006.07.020
M3 - 学術論文
C2 - 16962744
AN - SCOPUS:33947500831
SN - 0927-7765
VL - 56
SP - 188
EP - 196
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
IS - 1-2
ER -