Please use this identifier to cite or link to this item:
|Title:||Chemical modifications of inert organic monolayers with oxygen plasma for biosensor applications|
|Source:||Xue, C.-Y., Yang, K.-L. (2007-05-08). Chemical modifications of inert organic monolayers with oxygen plasma for biosensor applications. Langmuir 23 (10) : 5831-5835. ScholarBank@NUS Repository. https://doi.org/10.1021/la070076+|
|Abstract:||In this paper we present a study of using oxygen plasma for chemically modifying inert hydrocarbon self-assembled monolayers of octadecyltrichlorosilane (OTS-SAMs) and rendering active surfaces for protein immobilization. Detailed surface modification and protein immobilization were characterized by using ellipsometry, X-ray photoelectron spectroscopy (XPS), Fourier transform infrared - attenuated total reflectance spectroscopy, and fluorescence microscopy. Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O - C=O), and their compositions can be controlled by using different treatment times and powers. A short treatment time (∼1 s) and high power (10 W) can lead to a higher density of aldehyde groups, which can serve as linker groups for protein immobilization through the formation of Schiff bases with the amine groups of proteins. By using the fluorescence immunostaining method, we confirmed that human immunoglobulin (IgG) can be immobilized on a glass slide, only if the surface was decorated with OTS-SAMs and if the OTS-SAMs were pretreated with oxygen plasma. The protein immobilized on the oxygen-plasma-treated surface can only be recognized by using a highly specific antibody, FITC - anti-IgG, but not FITC - anti-biotin. © 2007 American Chemical Society.|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 13, 2018
WEB OF SCIENCETM
checked on Jan 10, 2018
checked on Feb 18, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.