AVS 57th International Symposium & Exhibition
    Biomaterial Interfaces Thursday Sessions
       Session BI-ThP

Paper BI-ThP2
Protein Resistant Oligo(ethylene glycol) Terminated Self-Assembled Monolayers of Thiols on Gold by Vapor Deposition in Vacuum

Thursday, October 21, 2010, 6:00 pm, Room Southwest Exhibit Hall

Session: Biomaterial Interfaces Poster Session
Presenter: A. Gölzhäuser, University of Bielefeld, Germany
Authors: L. Kankate, University of Bielefeld, Germany
H. Großmann, Johann Wolfgang Goethe-University, Germany
U. Werner, University of Bielefeld, Germany
R. Tampé, Johann Wolfgang Goethe-University, Germany
A. Turchanin, University of Bielefeld, Germany
A. Gölzhäuser, University of Bielefeld, Germany
Correspondent: Click to Email

Protein resistant oligo(ethylene glycol) terminated (OEG) self-assembled monolayers (SAMs) of thiols on gold are commonly used for suppression of nonspecific protein adsorption in biology and biotechnology. The standard preparation for these SAMs is the solution method (SM) that involves immersion of the gold surface in an OEG solution. Here we present the preparation of 11-(mercaptoundecyl)-triethylene glycol (HS(CH2)11(OCH2CH2)3OH) SAMs on gold surface by vapor deposition (VD) in vacuum. We compare the properties of SAMs prepared by VD and SM using X-ray photoelectron spectroscopy (XPS), polarisation modulation infrared reflection absorption spectroscopy (PM-IRRAS) and surface plasmon resonance (SPR) measurements. VD and SM SAMs exhibit similar packing density and show a similar resistance to the nonspecific adsorption of various proteins (bovine serum albumin, trypsin, and myoglobin) under physiological conditions. A very high sensitivity of the OEG SAMs to X-ray radiation is found, which allows tuning their protein resistance. These results show a new path to in situ engineering, analysis and patterning of protein resistant OEG SAMs by high vacuum and ultra high vacuum techniques.

[1] L. Kankate, H. Großmann, U. Werner, R. Tampé, A. Turchanin, A. Gölzhäuser, Biointerphases 5, 30 (2010)