Abstract

An optical method is presented for in the situ monitoring of biomolecular films via reflection microscopy on patterned substrates. The method is based on measuring the reflection coefficient of a composite consisting of a substrate, a patterned optical layer, the thin film to be monitored and the cover medium. The optical layer is patterned so that an array of squares is surrounded by the bare substrate. The reflectance difference between the optical layer squares and the bare substrate is the observable, whose fractional changes reveal the thickness of the film through a simple analytical expression. The periodic image is recorded by a digital microscope, and through Fourier transform techniques, the normalized differential reflectance of the patterned optical composite is calculated as the contrast factor of two dimensional bit map. The method is demonstrated by measuring a protein binding assay inside a microfluidic module placed under a microscope.

© 2013 OSA

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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
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    [CrossRef]
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    [CrossRef]
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    [CrossRef]
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    [CrossRef] [PubMed]
  11. P. Ihalainen and J. Peltonen, “Immobilization of streptavidin onto biotin-functionalized Langmuir-Schaefer binary monolayers chemisorbed on gold,” Sens. Actuat. B102(2), 207–218 (2004).
    [CrossRef]
  12. M. Zavali, “Direct Study of biomolecular interactions through white light reflection spectroscopy” Senior Thesis, University of Ioannina, Greece, (2006).

2012

X. W. Guo, “Surface plasmon resonance based biosensor technique: a review,” J Biophotonics5(7), 483–501 (2012).
[CrossRef] [PubMed]

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

2010

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

M. S. Luchansky and R. C. Bailey, “Silicon photonic microring resonators for quantitative cytokine detection and T-cell secretion analysis,” Anal. Chem.82(5), 1975–1981 (2010).
[CrossRef] [PubMed]

2007

2006

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

2004

P. Ihalainen and J. Peltonen, “Immobilization of streptavidin onto biotin-functionalized Langmuir-Schaefer binary monolayers chemisorbed on gold,” Sens. Actuat. B102(2), 207–218 (2004).
[CrossRef]

2002

S. Busse, V. Scheumann, B. Menges, and S. Mittler, “Sensitivity studies for specific binding reactions using the biotin/streptavidin system by evanescent optical methods,” Biosens. Bioelectron.17(8), 704–710 (2002).
[CrossRef] [PubMed]

2000

A. P. F. Turner, “Biochemistry. Biosensors--sense and sensitivity,” Science290(5495), 1315–1317 (2000).
[CrossRef] [PubMed]

1993

A. Brecht, G. Gauglitz, and J. Polster, “Interferometric immunoassay in a FIA-system - a sensitive and rapid approach in label-free immunosensing,” Biosens. Bioelectron.8(7-8), 387–392 (1993).
[CrossRef]

Bailey, R. C.

M. S. Luchansky and R. C. Bailey, “Silicon photonic microring resonators for quantitative cytokine detection and T-cell secretion analysis,” Anal. Chem.82(5), 1975–1981 (2010).
[CrossRef] [PubMed]

Beltsios, K.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Bockova, M.

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

Brecht, A.

A. Brecht, G. Gauglitz, and J. Polster, “Interferometric immunoassay in a FIA-system - a sensitive and rapid approach in label-free immunosensing,” Biosens. Bioelectron.8(7-8), 387–392 (1993).
[CrossRef]

Busse, S.

S. Busse, V. Scheumann, B. Menges, and S. Mittler, “Sensitivity studies for specific binding reactions using the biotin/streptavidin system by evanescent optical methods,” Biosens. Bioelectron.17(8), 704–710 (2002).
[CrossRef] [PubMed]

Dai, J.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Gauglitz, G.

A. Brecht, G. Gauglitz, and J. Polster, “Interferometric immunoassay in a FIA-system - a sensitive and rapid approach in label-free immunosensing,” Biosens. Bioelectron.8(7-8), 387–392 (1993).
[CrossRef]

Gregg, J. P.

Guo, X.

Guo, X. W.

X. W. Guo, “Surface plasmon resonance based biosensor technique: a review,” J Biophotonics5(7), 483–501 (2012).
[CrossRef] [PubMed]

He, L. P.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Herranz, S.

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

Homola, J.

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

Ihalainen, P.

P. Ihalainen and J. Peltonen, “Immobilization of streptavidin onto biotin-functionalized Langmuir-Schaefer binary monolayers chemisorbed on gold,” Sens. Actuat. B102(2), 207–218 (2004).
[CrossRef]

Jin, K. J.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Kakabakos, S. E.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Kitsara, M.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Lam, K. S.

Landry, J. P.

Lu, H. B.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Luchansky, M. S.

M. S. Luchansky and R. C. Bailey, “Silicon photonic microring resonators for quantitative cytokine detection and T-cell secretion analysis,” Anal. Chem.82(5), 1975–1981 (2010).
[CrossRef] [PubMed]

Marazuela, M. D.

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

Menges, B.

S. Busse, V. Scheumann, B. Menges, and S. Mittler, “Sensitivity studies for specific binding reactions using the biotin/streptavidin system by evanescent optical methods,” Biosens. Bioelectron.17(8), 704–710 (2002).
[CrossRef] [PubMed]

Misiakos, K.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Mittler, S.

S. Busse, V. Scheumann, B. Menges, and S. Mittler, “Sensitivity studies for specific binding reactions using the biotin/streptavidin system by evanescent optical methods,” Biosens. Bioelectron.17(8), 704–710 (2002).
[CrossRef] [PubMed]

Moreno-Bondi, M. C.

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

Peltonen, J.

P. Ihalainen and J. Peltonen, “Immobilization of streptavidin onto biotin-functionalized Langmuir-Schaefer binary monolayers chemisorbed on gold,” Sens. Actuat. B102(2), 207–218 (2004).
[CrossRef]

Petrou, P. S.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Polster, J.

A. Brecht, G. Gauglitz, and J. Polster, “Interferometric immunoassay in a FIA-system - a sensitive and rapid approach in label-free immunosensing,” Biosens. Bioelectron.8(7-8), 387–392 (1993).
[CrossRef]

Raptis, I.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Scheumann, V.

S. Busse, V. Scheumann, B. Menges, and S. Mittler, “Sensitivity studies for specific binding reactions using the biotin/streptavidin system by evanescent optical methods,” Biosens. Bioelectron.17(8), 704–710 (2002).
[CrossRef] [PubMed]

Sun, Y.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Sun, Y. S.

Turner, A. P. F.

A. P. F. Turner, “Biochemistry. Biosensors--sense and sensitivity,” Science290(5495), 1315–1317 (2000).
[CrossRef] [PubMed]

Wang, J. Y.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Yang, G. Z.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Zavali, M.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Zhu, X.

Anal. Bioanal. Chem.

S. Herranz, M. Bockova, M. D. Marazuela, J. Homola, and M. C. Moreno-Bondi, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Anal. Bioanal. Chem.398(6), 2625–2634 (2010).
[CrossRef] [PubMed]

Anal. Chem.

M. S. Luchansky and R. C. Bailey, “Silicon photonic microring resonators for quantitative cytokine detection and T-cell secretion analysis,” Anal. Chem.82(5), 1975–1981 (2010).
[CrossRef] [PubMed]

Appl. Opt.

Biosens. Bioelectron.

A. Brecht, G. Gauglitz, and J. Polster, “Interferometric immunoassay in a FIA-system - a sensitive and rapid approach in label-free immunosensing,” Biosens. Bioelectron.8(7-8), 387–392 (1993).
[CrossRef]

S. Busse, V. Scheumann, B. Menges, and S. Mittler, “Sensitivity studies for specific binding reactions using the biotin/streptavidin system by evanescent optical methods,” Biosens. Bioelectron.17(8), 704–710 (2002).
[CrossRef] [PubMed]

J Biophotonics

X. W. Guo, “Surface plasmon resonance based biosensor technique: a review,” J Biophotonics5(7), 483–501 (2012).
[CrossRef] [PubMed]

J. Appl. Phys.

J. Y. Wang, J. Dai, L. P. He, Y. Sun, H. B. Lu, K. J. Jin, and G. Z. Yang, “Label-free and real-time detections of the interactions of swine IgG with goat anti-swine IgG by oblique-incidence reflectivity difference technique,” J. Appl. Phys.112(6), 064702 (2012).
[CrossRef]

Micro & Nano Lett.

M. Zavali, P. S. Petrou, S. E. Kakabakos, M. Kitsara, I. Raptis, K. Beltsios, and K. Misiakos, “Label-free kinetic study of biomolecular interactions by white light reflectance spectroscopy,” Micro & Nano Lett.1(2), 94–98 (2006).
[CrossRef]

Science

A. P. F. Turner, “Biochemistry. Biosensors--sense and sensitivity,” Science290(5495), 1315–1317 (2000).
[CrossRef] [PubMed]

Sens. Actuat. B

P. Ihalainen and J. Peltonen, “Immobilization of streptavidin onto biotin-functionalized Langmuir-Schaefer binary monolayers chemisorbed on gold,” Sens. Actuat. B102(2), 207–218 (2004).
[CrossRef]

Other

M. Zavali, “Direct Study of biomolecular interactions through white light reflection spectroscopy” Senior Thesis, University of Ioannina, Greece, (2006).

O. S. Heavens, Optical Properties of Thin Solid Films (Dover Publications, 1991) Chap.4.

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