title: Factors that determine the protein resistance of oligoether self-assembled monolayers --internal hydrophilicity, terminal hydrophilicity, and lateral packing density.
abstract: Protein resistance of oligoether self-assembled monolayers (SAMs) on gold and silver surfaces has been investigated systematically to elucidate structural factors that determine whether a SAM will be able to resist protein adsorption. Oligo(ethylene glycol) (OEG)-, oligo(propylene glycol)-, and oligo(trimethylene glycol)-terminated alkanethiols with different chain lengths and alkyl termination were synthesized as monolayer constituents. The packing density and chemical composition of the SAMs were examined by XPS spectroscopy; the terminal hydrophilicity was characterized by contact angle measurements. IRRAS spectroscopy gave information about the chain conformation of specific monolayers; the amount of adsorbed protein as compared to alkanethiol monolayers was determined by ellipsometry. We found several factors that in combination or by themselves suppress the protein resistance of oligoether monolayers. Monolayers with a hydrophobic interior, such as those containing oligo(propylene glycol), show no protein resistance. The lateral compression of oligo(ethylene glycol) monolayers on silver generates more highly ordered monolayers and may cause decreased protein resistance, but does not necessarily lead to an all-trans chain conformation of the OEG moieties. Water contact angles higher than 70 degrees on gold or 65 degrees on silver reduce full protein resistance. We conclude that both internal and terminal hydrophilicity favor the protein resistance of an oligoether monolayer. It is suggested that the penetration of water molecules in the interior of the SAM is a necessary prerequisite for protein resistance. We discuss and summarize the various factors which are critical for the functionality of "inert" organic films.
authors.affiliation: Angewandte Physikalische Chemie, Universität Heidelberg, INF 253, D 69120 Heidelberg, Germany.
authors.forename: Sascha
authors.initials: S
authors.lastname: Herrwerth
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Eck
authors.forename: Sven
authors.initials: S
authors.lastname: Reinhardt
authors.forename: Michael
authors.initials: M
authors.lastname: Grunze
mesh_terms: D000327:Adsorption; D005340:Fibrinogen / Q000737:chemistry*; D006046:Gold / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D011092:Polyethylene Glycols / Q000737:chemistry*; D012834:Silver / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D013057:Spectrum Analysis / Q000379:methods; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D013438:Sulfhydryl Compounds; D012834:Silver; D011092:Polyethylene Glycols; D006046:Gold; D005340:Fibrinogen