Anti-biofouling properties of a telomer brush with pendent glucosylurea groups

A thiol-group-carrying telomer with pendent D-glucosylurea groups [poly(glucosylureaethyl methacrylate)-SH (PolyGUMA-SH)] was obtained by reversible addition-fragmentation chain-transfer (RAFT) polymerization of GUMA in the presence of 4,4'-azobis(4-cyanopentanoic acid) (initiator) and 4-cyanop...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 16 vom: 18. Aug., Seite 9361-8
1. Verfasser: Kitano, Hiromi (VerfasserIn)
Weitere Verfasser: Hayashi, Atsushi, Takakura, Hajime, Suzuki, Hisatomo, Kanayama, Naoki, Saruwatari, Yoshiyuki
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Colloids Methacrylates Polymers Sulfhydryl Compounds Gold 7440-57-5 glucosylurea 7GF386763Z mehr... Urea 8W8T17847W Glucose IY9XDZ35W2 2-(dimethylamino)ethyl methacrylate O0V97PV2G1
Beschreibung
Zusammenfassung:A thiol-group-carrying telomer with pendent D-glucosylurea groups [poly(glucosylureaethyl methacrylate)-SH (PolyGUMA-SH)] was obtained by reversible addition-fragmentation chain-transfer (RAFT) polymerization of GUMA in the presence of 4,4'-azobis(4-cyanopentanoic acid) (initiator) and 4-cyanopentanoic acid dithiobenzoate (chain-transfer agent) and subsequent reduction with NaBH4. The thiol-carrying telomer was accumulated on both a gold electrode and a colloidal gold-immobilized glass substrate as proven by cyclic voltammetry using hydroquinone as a probe, and the increase in absorbance at 550 nm was ascribable to localized surface plasmon resonance (LSPR), respectively. The adsorption of various proteins to the surface of the telomer brush was examined by the LSPR method, too. The PolyGUMA brush showed a significant resistance against nonspecific adsorption of proteins, such as lysozyme, bovine serum albumin, immunoglobulin G, and fibrinogen. Furthermore, sugar-binding proteins, concanavalin A (Con A, with an affinity for mannose and glucose) and wheat germ agglutinin (WGA, with an affinity for N-acetylglucosamine), were not adsorbed to the GUMA-carrying brush, which is in contrast with the prompt and distinct binding of these proteins to the telomer brushes composed of 2-methacryloyloxyethyl D-glucopyranoside (Con A) and 1-O-(6'-methacrylamido)hexyl-2-N-acetoamido-2-deoxy-D-glucopyranoside residues (WGA). The glucosylurea-group-carrying telomer brush prepared here might be quite useful to provide a "bio-inert (anti-biofouling)" surface in biomedical fields
Beschreibung:Date Completed 13.10.2009
Date Revised 16.11.2017
published: Print
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la9008625