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  Factors that determine the protein resistance of oligoether self-assembled monolayers --internal hydrophilicity, terminal hydrophilicity, and lateral packing density

Herrwerth, S., Eck, W., Reinhardt, S., & Grunze, M. (2003). Factors that determine the protein resistance of oligoether self-assembled monolayers --internal hydrophilicity, terminal hydrophilicity, and lateral packing density. Journal of the American Chemical Society, 125(31), 9359-9366. doi:10.1021/ja034820y.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-C124-C Version Permalink: https://hdl.handle.net/21.11116/0000-0001-C125-B
Genre: Journal Article

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 Creators:
Herrwerth, Sascha, Author
Eck, Wolfgang, Author
Reinhardt, Sven, Author
Grunze, Michael1, Author           
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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 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.

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Language(s): eng - English
 Dates: 2003-02-232003-07-15
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/ja034820y
URI: https://www.ncbi.nlm.nih.gov/pubmed/12889964
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Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 125 (31) Sequence Number: - Start / End Page: 9359 - 9366 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870