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Development of a plastic-based microfluidic immunosensor chip for detection of H1N1 influenza.

Lee KG, Lee TJ, Jeong SW, Choi HW, Heo NS, Park JY, Park TJ, Lee SJ - Sensors (Basel) (2012)

Bottom Line: A fluorescent dye-labeled antibody (Ab) was used for quantifying the concentration of Ab in the immunosensor chip using a fluorescent technique.For increasing the detection efficiency and reducing the errors, three chambers and three microchannels were designed in one microfluidic chip.This protocol could be applied to the diagnosis of other infectious diseases in a microfluidic device.

View Article: PubMed Central - PubMed

Affiliation: Center for Nanobio Integration & Convergence Engineering (NICE), National NanoFab Center, 291 Daehak-ro, Yuseong-gu, Daejeon 305-806, Korea. kglee@nnfc.re.kr

ABSTRACT
Lab-on-a-chip can provide convenient and accurate diagnosis tools. In this paper, a plastic-based microfluidic immunosensor chip for the diagnosis of swine flu (H1N1) was developed by immobilizing hemagglutinin antigen on a gold surface using a genetically engineered polypeptide. A fluorescent dye-labeled antibody (Ab) was used for quantifying the concentration of Ab in the immunosensor chip using a fluorescent technique. For increasing the detection efficiency and reducing the errors, three chambers and three microchannels were designed in one microfluidic chip. This protocol could be applied to the diagnosis of other infectious diseases in a microfluidic device.

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Related in: MedlinePlus

Molecular binding optimization of GBP-H1a fusion protein and its specific Ab with different concentrations. (A) Specific bindings of GBP-H1a fusion protein onto the gold surface. (B) Subsequent bindings of anti-H1 Ab. The bindings were started at 150 s and the unbound samples were washed at 750 s.
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f3-sensors-12-10810: Molecular binding optimization of GBP-H1a fusion protein and its specific Ab with different concentrations. (A) Specific bindings of GBP-H1a fusion protein onto the gold surface. (B) Subsequent bindings of anti-H1 Ab. The bindings were started at 150 s and the unbound samples were washed at 750 s.

Mentions: To investigate the sensing window of the fusion protein, different concentrations (6.25, 12.5, 25, 50, 100 and 200 μg/mL, respectively) of GBP-H1a fusion protein were immobilized onto the gold chip surface by surface plasmon resonance (SPR) microfluidics. A greater shift in resonance unit (RU) was observed by SPR analysis with increasing concentration of immobilized GBP-H1a fusion protein bound on the planar surface at various concentrations as shown in Figure 3(A). These results suggest that the SPR sensor with GBP-fusion protein implemented on the gold surface can be an effective system for biomolecular immobilization. Furthermore, the concentration of GBP-H1a fusion protein was fixed to 100 μg/mL due to its best immobilization concentration.


Development of a plastic-based microfluidic immunosensor chip for detection of H1N1 influenza.

Lee KG, Lee TJ, Jeong SW, Choi HW, Heo NS, Park JY, Park TJ, Lee SJ - Sensors (Basel) (2012)

Molecular binding optimization of GBP-H1a fusion protein and its specific Ab with different concentrations. (A) Specific bindings of GBP-H1a fusion protein onto the gold surface. (B) Subsequent bindings of anti-H1 Ab. The bindings were started at 150 s and the unbound samples were washed at 750 s.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3472858&req=5

f3-sensors-12-10810: Molecular binding optimization of GBP-H1a fusion protein and its specific Ab with different concentrations. (A) Specific bindings of GBP-H1a fusion protein onto the gold surface. (B) Subsequent bindings of anti-H1 Ab. The bindings were started at 150 s and the unbound samples were washed at 750 s.
Mentions: To investigate the sensing window of the fusion protein, different concentrations (6.25, 12.5, 25, 50, 100 and 200 μg/mL, respectively) of GBP-H1a fusion protein were immobilized onto the gold chip surface by surface plasmon resonance (SPR) microfluidics. A greater shift in resonance unit (RU) was observed by SPR analysis with increasing concentration of immobilized GBP-H1a fusion protein bound on the planar surface at various concentrations as shown in Figure 3(A). These results suggest that the SPR sensor with GBP-fusion protein implemented on the gold surface can be an effective system for biomolecular immobilization. Furthermore, the concentration of GBP-H1a fusion protein was fixed to 100 μg/mL due to its best immobilization concentration.

Bottom Line: A fluorescent dye-labeled antibody (Ab) was used for quantifying the concentration of Ab in the immunosensor chip using a fluorescent technique.For increasing the detection efficiency and reducing the errors, three chambers and three microchannels were designed in one microfluidic chip.This protocol could be applied to the diagnosis of other infectious diseases in a microfluidic device.

View Article: PubMed Central - PubMed

Affiliation: Center for Nanobio Integration & Convergence Engineering (NICE), National NanoFab Center, 291 Daehak-ro, Yuseong-gu, Daejeon 305-806, Korea. kglee@nnfc.re.kr

ABSTRACT
Lab-on-a-chip can provide convenient and accurate diagnosis tools. In this paper, a plastic-based microfluidic immunosensor chip for the diagnosis of swine flu (H1N1) was developed by immobilizing hemagglutinin antigen on a gold surface using a genetically engineered polypeptide. A fluorescent dye-labeled antibody (Ab) was used for quantifying the concentration of Ab in the immunosensor chip using a fluorescent technique. For increasing the detection efficiency and reducing the errors, three chambers and three microchannels were designed in one microfluidic chip. This protocol could be applied to the diagnosis of other infectious diseases in a microfluidic device.

Show MeSH
Related in: MedlinePlus