2007
DOI: 10.1088/0953-8984/19/39/395009
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Confocal imaging of protein distributions in porous silicon optical structures

Abstract: The performances of porous silicon optical biosensors depend strongly on the arrangement of the biological probes into their sponge-like structures: it is well known that in this case the sensing species do not fill the pores but instead cover their internal surface. In this paper, the direct imaging of labelled proteins into different porous silicon structures by using a confocal laser microscope is reported. The distribution of the biological matter in the nanostructured material follows a Gaussian behaviour… Show more

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Cited by 12 publications
(5 citation statements)
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“…Figure 8D quantifies the intensity profiles of the average fluorescence signal and it could be clearly seen that the labeled protein was distributed as a Gaussian function having its maximum value close to the center of the layer. This result further confirm that the protein was penetrated inside the pores (De Stefano and D'Auria, 2007 ).…”
Section: Resultssupporting
confidence: 81%
“…Figure 8D quantifies the intensity profiles of the average fluorescence signal and it could be clearly seen that the labeled protein was distributed as a Gaussian function having its maximum value close to the center of the layer. This result further confirm that the protein was penetrated inside the pores (De Stefano and D'Auria, 2007 ).…”
Section: Resultssupporting
confidence: 81%
“…The etching depth and accordingly the pore length can be simply controlled via the etching time [25,61]. Moreover, on demand, the porous matrix can be detached from the underlying silicon wafer after finishing the etching process rendering this porous structure particularly versatile for studies of nanopore-condensed matter [4,29,[62][63][64][65][66][67][68][69][70][71][72][73][74][75].…”
Section: Film Adsorption and Capillary Condensationmentioning
confidence: 99%
“…In this work, we evaluate mesoporous silicon microparticles as a nontoxic delivery system for the more effective delivery of anthelmintic protein Cry5B . Cry5B toxin is a large (140 kDa) protein composed of three distinct domains, with the overall dimensions of 85 × 65 × 45 Å 3 . , The pore dimensions in electrochemically generated mesoporous Si can be adjusted to a size adequate to admit this protein ,, but sufficiently small to inhibit the action of proteolytic enzymes. For this study, we investigated a partially oxidized form of pSi because the oxide surface has been shown to be compatible with sensitive proteins, , and the negatively charged surface allows concentration of positively charged proteins in the pores via electrostatic forces. , Furthermore, oxidized pSi has been shown to be stable under acidic conditions but readily dissolves at pH >7, which is advantageous for an oral route of delivery to the intestines. , …”
mentioning
confidence: 99%