Creation and control of defined protein patterns on glass: alkyl chain length controls stability

Abstract

Here we present a method for the production of defined protein patterns on glass using trimethoxysilane-terminated self-assembled monolayer (SAM) chemistry. The surfaces were characterized by infrared spectroscopy to determine the relationship between alkyl chain length and monolayer order and, in turn, the critical alkyl chain length required to produce a tightly packed SAM. Protein resistance studies, which incorporated a glycol region into the monomer, further highlighted the importance of alkane chain length within the monolayer, as increased chain length was necessary to generate protein resistant regions that persisted for more than a few days. The long-chain trimethoxysilane-terminated monomers that we have developed are stable, can be purified using standard silicon gel chromatography, and can be easily patterned using methods developed for other SAMs. As a result, these monomers and the resulting monolayers produced from them provide a method for the functionalization of a wide variety of oxide substrates, including ordinary glass, which has enormous advantages over previous glycol-terminated trichlorosilane monomers.