immobilizedproteinsurfacesusing.PDF

J. Biochem. Biophys. Methods 58 (2004) 67–74 /locate/jbbm Reduced nonspecific adsorption on covalently immobilized protein surfaces using poly(ethylene oxide) containing blocking agents a,*, Kristien Bonroya a Filip Frederix , Gunter Reekmans , Wim Laureyn a a b , Andrew Campitelli , Mikhael A. Abramov , Wim Dehaenb, Guido Maesb a IMEC, MCP-BIO, Kapeldreef 75, B-3001 Louvain, Belgium b K.U. Leuven, Department of Chemistry, Celestijnenlaan 200F, B-3001, Louvain, Belgium Received 17 June 2003; received in revised form 17 June 2003; accepted 13 July 2003 Abstract In a number of applications, e.g. DNA/protein micro-array technology, enzyme-linked immunosorbent assay (ELISA) technology or surface plasmon resonance (SPR) technology, the covalent coupling of proteins to surfaces is required. Following the covalent coupling of proteins, the remaining reactive groups should be blocked in order to avoid covalent binding of the analyte to the reactive surface. To this end, preferably blocking agents containing groups that avoid nonspecific adsorption should be used. These blocking agents are typically ethanolamine and cysteine for protein coupling via amino groups and thiol groups, respectively. This report presents novel blocking agents containing poly(ethylene oxide) (PEO) groups. These blocking agents show enhanced qualities to avoid nonspecific adsorption and can therefore have advantages in versatile protein-surface techn