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  Temperature dependence of the protein resistance of poly- and oligo(ethylene glycol)-terminated alkanethiolate monolayers

Schwendel, D., Dahint, R., Herrwerth, S., Schloerholz, M., Eck, W., & Grunze, M. (2001). Temperature dependence of the protein resistance of poly- and oligo(ethylene glycol)-terminated alkanethiolate monolayers. Langmuir, 17(19), 5717-5720. doi:10.1021/la010576h.

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Schwendel, Dirk, Author
Dahint, Reiner, Author
Herrwerth, Sascha, Author
Schloerholz, Matthias, Author
Eck, Wolfgang, Author
Grunze, Michael1, Author           
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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 Abstract: Fourier transform infrared reflection absorption spectroscopy (FT-IRRAS) has been used to study the protein resistance of poly- and oligo(ethylene glycol) (PEG and OEG) terminated alkanethiolate self-assembled monolayers (SAMs) on Au and Ag in the temperature range from 0 to 85 °C. These experiments extend previous room-temperature studies by Harder et al.1 who related the protein adsorption characteristics of OEG-SAMs to the lateral density and corresponding molecular conformation of the ethylene glycol (EG) moieties in the film. In addition to the short oligomer OEG-SAMs, we investigated PEG-derivatized alkanethiolate monolayers with an average chain length of 45 EG units and a mean molecular mass of 2000 g/mol (PEG2000). We observe that films, which are protein resistant at room temperature, maintain their protein repulsive characteristics up to 85 °C but may adsorb significant amounts of protein if the temperature is lowered.

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Language(s): eng - English
 Dates: 2001-07-022001-04-192001
 Publication Status: Issued
 Pages: 4
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 Rev. Type: Peer
 Identifiers: DOI: 10.1021/la010576h
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Title: Langmuir
Source Genre: Journal
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Publ. Info: Columbus, OH : American Chemical Society
Pages: - Volume / Issue: 17 (19) Sequence Number: - Start / End Page: 5717 - 5720 Identifier: ISSN: 0743-7463
CoNE: https://pure.mpg.de/cone/journals/resource/954925541194