Protein resistant oligo(ethylene glycol) terminated self-assembled monolayers of thiols on gold by vapor deposition in vacuum
Author(s) -
Laxman Kankate,
U. Werner,
Andrey Turchanin,
Armin Gölzhäuser,
H. Großmann,
Robert Tampé
Publication year - 2010
Publication title -
biointerphases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.633
H-Index - 45
eISSN - 1934-8630
pISSN - 1559-4106
DOI - 10.1116/1.3407483
Subject(s) - chemistry , ethylene glycol , monolayer , self assembled monolayer , protein adsorption , contact angle , x ray photoelectron spectroscopy , surface plasmon resonance , chemical vapor deposition , adsorption , infrared spectroscopy , chemical engineering , analytical chemistry (journal) , nanotechnology , organic chemistry , materials science , nanoparticle , biochemistry , engineering
Protein resistant oligo(ethylene glycol) (OEG) terminated 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 the authors present the preparation of 11-(mercaptoundecyl)-triethylene glycol [HS(CH(2))(11)(OCH(2)CH(2))(3)OH] SAMs on gold surface by vapor deposition (VD) in vacuum. They compare the properties of SAMs prepared by VD and SM using x-ray photoelectron spectroscopy (XPS), polarization modulation infrared reflection absorption spectroscopy, and surface plasmon resonance 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 ultrahigh vacuum techniques.
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