Highly Selective Protein Patterning on Gold-Silicon Substrates for Biosensor Applications

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dc.contributor.author Veiseh, M
dc.contributor.author Zareie, HM
dc.contributor.author Zhang, M
dc.date.accessioned 2009-06-26T04:10:52Z
dc.date.issued 2002-01
dc.identifier.citation Langmuir, 2002, 18 (17), pp. 6671 - 6678
dc.identifier.issn 0743-7463
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/578
dc.description.abstract Proteins were precisely patterned on 2D sensor surfaces using photolithography and chemical selectivity. Microarrays of gold squares were fabricated on silicon substrates. The gold regions were modified with mixed COOH-terminated self-assembled monolayers (SAMs) to have a high affinity for the desired proteins or peptides. The silicon regions were modified with polyethylene glycol (PEG) by silanization to provide a high resistivity to protein adsorption. Protein surface coverage was visualized by fluorescence microscopy and atomic force microscopy (AFM). AFM was also used for studying protein morphology to understand the interaction of proteins with SAMs at the molecular level. Proteins and peptides immobilized on SAMs were examined by Fourier transform infrared (FTIR) spectroscopy. Contact angle measurements for surface wettability were conducted to confirm the success of the surface modification reactions. Protein resistance by the PEGs immobilized on bare silicon substrates and on the silicon regions of gold-patterned silicon substrates was compared, and it was found that the latter has a higher resistivity to protein adsorption. Both fluorescence and high-resolution AFM images indicated that bovine serum albumin (BSA) and fibronectin molecules formed a densely packed layer on the gold regions of the patterned substrates, while the immunoglobulin's (IgG) coverage was low. Specific antigen-antibody binding (BSA-anti-BSA) was studied using the surface plasmon resonance (SPR) technique for characterizing the bioactivity of the antigen attached to the gold substrates. The SPR results showed that the BSA proteins bound covalently to the gold surfaces have a much better bioactivity than those bound physically. This study suggests that protein or peptide, molecular structures, and the immobilization technique influence the coverage, morphology, and bioactivity of the attached proteins on the substrates which is crucial to the operational behavior of biosensors.
dc.publisher American Chemical Society
dc.relation.isbasedon 10.1021/la025529j
dc.title Highly Selective Protein Patterning on Gold-Silicon Substrates for Biosensor Applications
dc.type Journal Article
dc.description.version Published
dc.parent Langmuir
dc.journal.volume 17
dc.journal.volume 18
dc.journal.number 17 en_US
dc.publocation Washington DC, USA en_US
dc.identifier.startpage 6671 en_US
dc.identifier.endpage 6678 en_US
dc.cauo.name SCI.Physics and Advanced Materials en_US
dc.conference Verified OK en_US
dc.for 0303 Macromolecular and Materials Chemistry
dc.for 0306 Physical Chemistry (Incl. Structural)
dc.for 1007 Nanotechnology
dc.personcode 030414
dc.percentage 70 en_US
dc.classification.name Nanotechnology en_US
dc.classification.type FOR-08 en_US
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc false
utslib.collection.history General Collection (ID: 346) [2015-05-15T14:11:13+10:00]
utslib.collection.history School of Physics and Advanced Materials (ID: 343)
utslib.collection.history Closed (ID: 3)

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