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Formation, Characterization, Protein Resistance, and Reactivity of Cl3Si(CH2)11(OCH2CH2)3OH Self-Assembled Monolayers Jiehyun Seong, Seok-Won Lee, and Paul E. Laibinis Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, U.S.A. ABSTRACT We report a method for generating tri(ethylene glycol)-terminated-n-alkyltrichlorosiloxane monolayers on SiO2 surfaces. These chemisorbed films, with a thickess of ~2-3 nm, provide an oligo(ethylene glycol) surface that reduces the nonspecific adsorption of proteins and hydroxyl attachment sites for covalently immobilizing biomolecules to the substrate. These monomolecular films were formed by adsorbing an acetoxy-tri(ethylene glycol)-terminated n-alkyltrichlorosilane, CH3(C=O)O(CH2CH2O)3(CH2)11SiCl3, onto glass and Si/SiO2 substrates, where the terminal acetate provided a protecting group for the hydroxyl functionality during selfassembly of the film. After formation of the monolayer, the acetate functionality was reduced chemically to form films exposing a covalently attached -(OCH2CH2)3OH terminus at a density of ~3×1014 molecules/cm2. Protein adsorption studies verified that the films exhibited notable resistances against the non-specific adsorption of various proteins. Chemical modification of the -(OCH2CH2)3OH surface with protein A provided a non-adsorbing surface for selective immobilization of immunoglobulins.

INTRODUCTION The construction of a variety of solid-state devices that interface fabricated systems with biological components or systems requires methods for assembling biomolecules on their surface in controlled ways. Examples include biosensors, chip-based diagnostic assays, and biomaterials used for implants and tissue engineering.1-4 A key issue in the design of analytical devices that contact biomolecules is that the non-specific adsorption of biological species, particularly proteins, can hinder their performance. For example, the unwanted adsorption of proteins and other species can hinder or alter the selective adsorption of agents to be analyzed, disturb the binding characteristics of immobilized receptor agents used in sensing, and introduce defects in patterned surfaces used in array-based assays. The structural integrity of immobilized biological species are greatly affected by their interactions with the underlying surface, where effects that cause non-specific adsorption can alter their activity and binding abilities as a result of structural changes effected by surface effects. A key need is the ability to have ”inert” surfaces that minimize unwanted adsorption events and allow the immobilization of biomolecules. In a previous paper, we detailed the preparation of self-assembled monolayer coatings by the adsorption of CH3O(CH2CH2O)2,3(CH2)11SiCl3 onto glass and Si/SiO2 substrates.5 The resulting chemisorbed films, approximately 2-3 nm in thickness, expressed a densely packed methoxycapped oligo(ethylene glycol) surface that dramatically retards the non-specific adsorption of various proteins. The methoxy

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