Bovine serum albumin adsorption on functionalized porous silicon surfaces

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DOIResolve DOI: http://doi.org/10.1117/12.567386
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TypeArticle
Proceedings titlePhotonics North 2004: Photonic Applications in Astronomy, Biomedicine, Imaging, Materials Processing, and Education
Series titleProceedings of SPIE; Volume 5578
ConferencePhotonics North 2004: Photonic Alications in Astronomy, Biomedicine, Imaging, Materials Processing, and Education, 27 September 2004, Ottawa, Canada
ISSN0277-786X
ISBN081945527X
Pages99106; # of pages: 8
AbstractThe large surface area within porous Si (pSi) and its strong room temperature photoluminescence (PL) make it an ideal host for biological sensors. In particular, the development of pSi-based optical sensors for DNA, enzyme and other biochemical molecules have become of great interest. Here, we demonstrate that the in-situ monitoring of the pSi PL behaviour can be used as a positive identification of bovine serum albumin (BSA) protein adsorption inside the porous matrix. Electrochemically prepared pSi films were first functionalized with undecylenic acid to produce an organic monolayer covalently attached to the porous silicon surfaces. The acid terminal group also provided favourable BSA binding sites on the pSi matrix sidewalls. In-situ PL spectra showed a gradual red shift (up to 12 meV) in the PL peak energy due to the protein incorporation into the porous matrix. The PL then exhibited a continuous blue shift after saturation of the protein molecules in the pores. This blue shift of the PL peak frequency and a steady increase in the PL intensity is evidence of surface oxidation. Comparing the specular reflectance obtained by Fourier transform infrared spectroscopy (FTIR) before and after BSA incubation confirmed the adsorption of protein in the pSi matrix.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Microstructural Sciences
Peer reviewedNo
NRC number1392
NPARC number12346627
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Record identifier60b997dd-85ee-4af6-bdef-b22047915597
Record created2009-09-17
Record modified2017-09-13
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