Protein-resistant poly(poly(ethylene glycol) monomethacrylate)-graft-Si(100), or Si-g-P(PEGMA) hybrids, were prepared via surface-initiated atom transfer radical polymerization (ATRP) of the poly(ethylene glycol)monomethacrylate (PEGMA) macromonomer from the hydrogen-terminated Si(100) surface (Si-H surface). The resultant robust Si-C bonded P(PEGMA) brushes can be further functionalized by the immobilization of human immunoglobulin (IgG) protein via different strategies, namely, the direct use of the alkyl halide chain ends preserved throughout the ATRP process and the postmodification of the hydroxyl side chains with by 1,1'-carbonyldiimidazole (CDI) or succinic anhydride (SA). The CDI exhibited a higher efficiency in activating the hydroxyl groups for coupling proteins. The surface density of the immobilized protein above 2.5 mu g/cm(2) could be readily achieved. The distribution of active protein-docking sites on the Si-C bonded P(PEGMA) brushes can be also controlled by controlling the brush length. The resulting IgG-coupled Si-g-P(PEGMA) hybrid surface interacts only and specifically with the anti-IgG protein, while the dense P(PEGMA) brushes effectively prevent nonspecific protein binding and fouling. The simple concomitant incorporation of protein-resistant P(PEGMA) brushes and highly specific and active protein onto silicon surfaces via robust Si-C bonding should readily endow the silicon substrates with new and interesting properties for applications in silicon-based protein sensors or microarrays.