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

Schwendel, Dirk; Dahint, Reiner; Herrwerth, Sascha; Schloerholz, Matthias; Eck, Wolfgang; Grunze, Michael

doi:10.1021/la010576h

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

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Grunze, Michael
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-0001-BDF1-A

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.