Please use this identifier to cite or link to this item: https://doi.org/10.1021/la070076+
DC FieldValue
dc.titleChemical modifications of inert organic monolayers with oxygen plasma for biosensor applications
dc.contributor.authorXue, C.-Y.
dc.contributor.authorYang, K.-L.
dc.date.accessioned2014-06-17T07:37:12Z
dc.date.available2014-06-17T07:37:12Z
dc.date.issued2007-05-08
dc.identifier.citationXue, 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+
dc.identifier.issn07437463
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/63586
dc.description.abstractIn 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/la070076+
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1021/la070076+
dc.description.sourcetitleLangmuir
dc.description.volume23
dc.description.issue10
dc.description.page5831-5835
dc.description.codenLANGD
dc.identifier.isiut000246071800090
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