title: Resistance of surface-confined telomers with pendent glucosylurea groups against non-specific adsorption of proteins.
abstract: 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.
authors.affiliation: Department of Applied Chemistry, Graduate School of Science and Engineering, University of Toyama, Toyama 930-8555, Japan. kitano@eng.u-toyama.ac.jp
authors.forename: Hiromi
authors.initials: H
authors.lastname: Kitano
authors.forename: Makoto
authors.initials: M
authors.lastname: Gemmei-Ide
authors.forename: Yasutaka
authors.initials: Y
authors.lastname: Anraku
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Saruwatari
mesh_terms: D000327:Adsorption; D003102:Colloids / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D004563:Electrochemistry / Q000379:methods; D005898:Glass / Q000737:chemistry; D005947:Glucose / Q000031:analogs & derivatives* / Q000737:chemistry; D006046:Gold / Q000737:chemistry; D006873:Hydroquinones / Q000737:chemistry; D007700:Kinetics; D008689:Methacrylates / Q000737:chemistry; D008956:Models, Chemical; D015394:Molecular Structure; D008970:Molecular Weight; D009391:Nephelometry and Turbidimetry; D011108:Polymers / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013053:Spectrophotometry; D013379:Substrate Specificity; D020349:Surface Plasmon Resonance; D013499:Surface Properties; D014508:Urea / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D003102:Colloids; D004220:Disulfides; D006873:Hydroquinones; D008689:Methacrylates; D011108:Polymers; D011506:Proteins; D006046:Gold; C036060:glucosylurea; D014508:Urea; D005947:Glucose; C031927:hydroquinone