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Virtual Journal for Biomedical Optics

Virtual Journal for Biomedical Optics

| EXPLORING THE INTERFACE OF LIGHT AND BIOMEDICINE

  • Editors: Andrew Dunn and Anthony Durkin
  • Vol. 8, Iss. 6 — Jun. 27, 2013
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Selective detection of sub-atto-molar Streptavidin in 1013-fold impure sample using photonic crystal nanolaser sensors

Shoji Hachuda, Shota Otsuka, Shota Kita, Toshinari Isono, Michimasa Narimatsu, Keisuke Watanabe, Yoshio Goshima, and Toshihiko Baba  »View Author Affiliations


Optics Express, Vol. 21, Issue 10, pp. 12815-12821 (2013)
http://dx.doi.org/10.1364/OE.21.012815


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Abstract

Biosensors selectively detecting a very small amount of biomarker protein in human blood are desired for early and reliable diagnoses of severe diseases. This paper reports the detection of protein (streptavidin: SA) in ultra-low concentration, with an ultra-high selectivity against contaminants, using photonic crystal nanolasers. For biotin-modified nanolasers in pure water with SA, an extremely-low detection limit of 16 zM is evaluated. Even in a mixture with 1 μM bovine serum albumin as the contaminant, 100 zM SA is detected, meaning a selectivity of 1013. These are remarkable capabilities that are promising for practical biosensing in the medical applications mentioned above.

© 2013 OSA

1. Introduction

Identification of severe diseases and advanced medical diagnoses are of increasing importance in aging societies [1

1. G.-J. Zhang, Z. H. H. Luo, M. J. Huang, J. J. Ang, T. G. Kang, and H. Ji, “An integrated chip for rapid, sensitive, and multiplexed detection of cardiac biomarkers from fingerprick blood,” Biosens. Bioelectron. 28(1), 459–463 (2011). [CrossRef] [PubMed]

], and therefore daily examinations of diagnostic biomarkers in blood and humor will have long demands. Although some easily-detectable biomarkers are already being serviced in health clinics, low-cost and high-throughput detection of very small amounts of specific biomarkers suitable for earlier and more reliable diagnoses is still a challenge [2

2. Y. D. Ivanov, V. M. Govorun, V. A. Bykov, and A. I. Archakov, “Nanotechnologies in proteomics,” Proteomics 6(5), 1399–1414 (2006). [CrossRef] [PubMed]

]. Common immunological methods such as enzyme-linked immunosorbent assay allow a detection limit (DL) of pM order [3

3. R. Wiese, Y. Belosludtsev, T. Powdrill, P. Thompson, and M. Hogan, “Simultaneous multianalyte ELISA performed on a microarray platform,” Clin. Chem. 47(8), 1451–1457 (2001). [PubMed]

], which barely meets the requirement for these biomarkers, and yet has problems that they need time-consuming functionalization procedures of fluorescent labels where the labels themselves are suspected to change the original properties of the biomarkers. As label-free methods, photonic sensors [4

4. B. J. Luff, J. S. Wilkinson, J. Piehler, U. Hollenbach, J. Ingenhoff, and N. Fabricius, “Integrated optical Mach-Zehnder biosensor,” J. Lightwave Technol. 16(4), 583–592 (1998). [CrossRef]

10

10. F. Vollmer and L. Yang, “Label-free detection with high-Q microcavities: a review of biosensing mechanisms for integrated devices,” Nanophotonics 1(3–4), 267–291 (2012).

] and those based on other physical parameters [1

1. G.-J. Zhang, Z. H. H. Luo, M. J. Huang, J. J. Ang, T. G. Kang, and H. Ji, “An integrated chip for rapid, sensitive, and multiplexed detection of cardiac biomarkers from fingerprick blood,” Biosens. Bioelectron. 28(1), 459–463 (2011). [CrossRef] [PubMed]

,11

11. M. G. von Muhlen, N. D. Brault, S. M. Knudsen, S. Y. Jiang, and S. R. Manalis, “Label-free biomarker sensing in undiluted serum with suspended microchannel resonators,” Anal. Chem. 82(5), 1905–1910 (2010). [CrossRef] [PubMed]

,12

12. M. M. A. Hakim, M. Lombardini, K. Sun, F. Giustiniano, P. L. Roach, D. E. Davies, P. H. Howarth, M. R. R. de Planque, H. Morgan, and P. Ashburn, “Thin film polycrystalline silicon nanowire biosensors,” Nano Lett. 12(4), 1868–1872 (2012). [CrossRef] [PubMed]

] have been developed. However, none of them simultaneously satisfy all the requirements of practical medical sensors: low cost, disposable use, simple procedure, high sensitivity, and high selectivity against contaminants.

In this paper, we present remarkably high-performance biosensing using photonic crystal (PC) nanolasers. The PC consists of GaInAsP semiconductor thin membrane with periodic airholes (PC slab) and some non-periodic airholes as a nanocavity [13

13. S. Kita, K. Nozaki, S. Hachuda, H. Watanabe, Y. Saito, S. Otsuka, T. Nakada, Y. Arita, and T. Baba, “Photonic crystal point-shift nanolaser with and without nanoslots −−− design, fabrication, lasing and sensing characteristics,” IEEE J. Sel. Top. Quantum Electron. 17(6), 1632–1647 (2011). [CrossRef]

]. Since its total area is no larger than 20 × 20 μm2, high-throughput low-cost fabrication and production will be feasible even using e-beam lithography. It is easily operated by room-temperature photopumping using a standard micro-photoluminescence (μ-PL) setup [13

13. S. Kita, K. Nozaki, S. Hachuda, H. Watanabe, Y. Saito, S. Otsuka, T. Nakada, Y. Arita, and T. Baba, “Photonic crystal point-shift nanolaser with and without nanoslots −−− design, fabrication, lasing and sensing characteristics,” IEEE J. Sel. Top. Quantum Electron. 17(6), 1632–1647 (2011). [CrossRef]

15

15. T. W. Lu, P. T. Lin, K. U. Sio, and P. T. Lee, “Optical sensing of square lattice photonic crystal point-shifted nanocavity for protein adsorption detection,” Appl. Phys. Lett. 96(21), 213702 (2010). [CrossRef]

]. In this device, the evanescent field of the laser mode penetrates outwards from the PC slab, and the laser wavelength is changed by the environmental index, which is the principle of the sensing. In addition, incorporating a nanoslot (NS) [13

13. S. Kita, K. Nozaki, S. Hachuda, H. Watanabe, Y. Saito, S. Otsuka, T. Nakada, Y. Arita, and T. Baba, “Photonic crystal point-shift nanolaser with and without nanoslots −−− design, fabrication, lasing and sensing characteristics,” IEEE J. Sel. Top. Quantum Electron. 17(6), 1632–1647 (2011). [CrossRef]

,16

16. J. T. Robinson, C. Manolatou, L. Chen, and M. Lipson, “Ultrasmall mode volumes in dielectric optical microcavities,” Phys. Rev. Lett. 95(14), 143901 (2005). [CrossRef] [PubMed]

,17

17. S. Kita, S. Hachuda, K. Nozaki, and T. Baba, “Nanoslot laser,” Appl. Phys. Lett. 97(16), 161108 (2010). [CrossRef]

] into the nanolaser enhances the localization of the laser mode in water and improves the sensitivity. The localization also improves the thermal stability because the positive thermo-optic effect in semiconductors is canceled by the negative effect in water. This suppresses the spectral chirping due to heating and greatly narrows the spectrum, resulting in higher resolution of the sensing. Using the NS nanolaser, we have detected bovine serum albumin (BSA) of 255 fM concentration [18

18. S. Kita, S. Hachuda, S. Otsuka, T. Endo, Y. Imai, Y. Nishijima, H. Misawa, and T. Baba, “Super-sensitivity in label-free protein sensing using a nanoslot nanolaser,” Opt. Express 19(18), 17683–17690 (2011). [CrossRef] [PubMed]

], which means 3 − 4 orders higher sensitivity than that of common surface plasmon resonance (SPR) sensors [6

6. W. C. Law, K. T. Yong, A. Baev, R. Hu, and P. N. Prasad, “Nanoparticle enhanced surface plasmon resonance biosensing: application of gold nanorods,” Opt. Express 17(21), 19041–19046 (2009). [CrossRef] [PubMed]

]. In this paper, we demonstrate an even higher sensitivity for biotin-streptavidin (SA) specific binding and detection with an ultra-high selectivity against BSA as the contaminant. Consequently, we show that this device satisfies potentially all the above requirements for practical medical sensors.

2. Device and method

PC nanolasers are fabricated on a 180 nm thick GaInAsP quantum-well active layer epitaxially grown on (100) InP substrate, as shown in Fig. 1
Fig. 1 Optical micrograph (left) and scanning electron micrograph (right) of GaInAsP NS PC nanolasers. Dark and bright areas of the left picture are those with lower InP removed and remained. Diameter of airholes inside dotted lines in the right picture is reduced from 2r to 2r’.
. We employ the simple process of e-beam lithography and HI inductively coupled plasma etching for making holes into the GaInAsP layer and HCl etching of InP beneath the holes to form the air-bridge structure. In this experiment, we prepared devices with and without a NS (NS width wNS = 20 − 80 nm) at the center of the cavity. The basic cavity structure is H0-type consisting of four shifted airholes [13

13. S. Kita, K. Nozaki, S. Hachuda, H. Watanabe, Y. Saito, S. Otsuka, T. Nakada, Y. Arita, and T. Baba, “Photonic crystal point-shift nanolaser with and without nanoslots −−− design, fabrication, lasing and sensing characteristics,” IEEE J. Sel. Top. Quantum Electron. 17(6), 1632–1647 (2011). [CrossRef]

]. The lattice constant a = 500 nm, airhole diameter 2r = 220 nm, and airhole shifts sx = 120 nm and sy = 80 nm. The periodic modification (airhole diameter 2r’ = 190 − 210 nm inside dotted lines) is added to enhance the vertical emission and enable easy detection in our setup [19

19. M. Narimatsu, S. Kita, H. Abe, and T. Baba, “Enhancement of vertical emission in photonic crystal nanolasers,” Appl. Phys. Lett. 100(12), 121117 (2012). [CrossRef]

]. Such devices are integrated in a 4 × 4 arrayed configuration within a footprint of less than 100 × 100 μm2. In one array of NS devices, wNS is varied so that we can evaluate sensor signals from various designs.

In the sensing experiment, the device chip is first thermally pre-oxidized at 180°C for one hour. If we do not this, GaInAsP surfaces are thermally oxidized during the laser operation in water. This reduces the effective index of the laser mode and results in the wavelength blueshift, which obscures the redshift due to the adsorption of proteins. The pre-oxidization is effective for suppressing additional oxidation in brief measurement. In addition, we recently found that the oxidation can be suppressed completely by coating the device with a transparent film. The detail on this matter is presented elsewhere [20

20. K. Watanabe, S. Hachuda, T. Isono, and T. Baba, “Photonic crystal nanolaser sensors with ALD coating”, Conference on Laser & Electro-Opt. Pacific Rim (CLEO) and Optoelectronic & Commun. Conf. / Photonics Switching (2013), paper TuJ2–2.

]. Therefore, it will not be a problem even in future experiments. Secondly, the device surface is treated to be hydrophilic in O2 plasma and functionalized with amino group in dehydrate toluene mixed with 0.05% 3-aminopropyl triethoxysilane (APTES) [21

21. T. Isono, H. Tanaka, and T. Ogino, ““Effect of chemical modification of the substrate surface on supported lipid bilayer formation,” e-J. Surf. Sci. Nanotech. 5, 99–102 (2007).

] for 5 min, and also with biotinylation in water mixed with 50 mM water-soluble carbodiimide (WSC) [22

22. N. Nakajima and Y. Ikada, “Mechanism of amide formation by carbodiimide for bioconjugation in aqueous media,” Bioconjug. Chem. 6(1), 123–130 (1995). [CrossRef] [PubMed]

] and 50 μg/ml biotin for one hour. Then, the chip is soaked in a sample liquid for 5 min, where the sample is a mixture of pure water, SA (concentrations of 0 – 100 pM), BSA (0 − 10 μM), and 0.1% surfactant Tween 20 [23

23. S. Mao, G. H. Lu, K. H. Yu, Z. Bo, and J. H. Chen, “Specific protein detection using thermally reduced graphene oxide sheet decorated with gold nanoparticle-antibody conjugates,” Adv. Mater. 22(32), 3521–3526 (2010). [CrossRef] [PubMed]

]. Both the specific adsorption of biotin-SA and non-specific adsorption of BSA can occur, as shown in Fig. 2
Fig. 2 Schematic of biotin-SA binding in impure sample.
, and the surfactant is expected to suppress the non-specific one. Finally the chip is rinsed by pure water, soaked in fresh pure water, and each device is photopumped at λ = 0.98 μm one by one through a μ-PL setup with a computer-controlled stage. The laser emission is coupled into optical fiber and its wavelength is measured using optical spectrum analyzer (OSA), Advantest Q8383 (resolution limit: 100 pm) or Q8384 (10 pm). Pulsed pumping (duty ratio = 200) is employed to avoid excess heating and further oxidation. In general, the laser wavelength redshifts with the adsorption. Wavelength shifts Δλ of the 16 devices (sometimes less than 16 when some devices do not emit enough power for the spectral analysis) are used for statistical evaluations such as averaging, confidence interval and t-test.

3. Results and discussion

First, we detected the biotin-SA binding in the absence of BSA and Tween 20. Here, samples of various SA concentrations were prepared by repeatedly pipetting and diluting the SA solution. To avoid any contaminations, the tip of the pipetter was replaced by a new one every time. We confirmed from the absorbance of dye-functionalized proteins that the protein concentration was diluted reasonably in this procedure at least in the μM regime (nM and lower concentrations are difficult to quantify in this method). The detection measurement was done in water, as aforementioned, after soaking the chip in each sample from low-concentration side and rinsing in pure water. When the above procedure of the soaking, rinsing, and measurement using Q8384 was repeated only with pure water not including SA, Δλ was less than 60 pm. We regard it as a noise level affected by the fluctuation in the measurement condition. Incidentally, we did not use buffer solutions including salt ions in this experiment to avoid the etching of the device surface. Similarly to the oxidation, such etching causes the wavelength blueshift and obscures the sensing. Since the aforementioned film coating also suppresses the etching completely, it will not be a problem even in buffer solutions in future experiments.

Next, we detected the biotin-SA binding in the presence of BSA and Tween 20. Here, surfactant Tween 20 hydrophilizes all the surfaces of proteins and devices. So it suppresses the non-specific adsorption of BSA, while does not disturb the biotin-SA binding as it desorbs from SA on this condition. Figure 4
Fig. 4 Wavelength shifts due to adsorption of SA in impure samples. (a) Laser spectra of 16 devices under three different conditions. Some spectra for #6 and #10 were missing in the automatic measurement, which might be due to position errors of pump light and weak emission intensity from nanolasers. (b) Average Δλ due to the adsorption of SA in impure samples with three different concentration BSA as impurities. Red and blue plots show those with and without biotin, respectively. Error bars indicate the range for 95% confidence interval.
summarizes the average Δλ with different SA concentrations in the presence of three different concentrations of BSA as the contaminant. Results in the absence of SA do not exhibit significant difference depending on the presence of biotin. When the BSA concentration is 100 nM, Δλ increases with increasing SA concentration only with the biotin; it was negligible without biotin. This indicates that biotin-SA specific binding occurs. When the BSA concentration is 1 μM, almost similar results are observed, although Δλ overall increased for both with and without biotin. This increase shouldbe due to the increase in the non-specific physisorption of BSA even with Tween 20 because of the very high concentration of BSA. Here, BSA might be adsorbed on the device surface as multi-layers and prohibits SA adsorption. This background noise increased more and obscured the main signal from the biotin-SA binding when the BSA concentration was 10 μM. Here we can see the gradual decrease in Δλ with increasing the SA concentration. This might also be due to the aforementioned oxidation of the device after repeated measurements. Thus we confirmed that the biotin-SA adsorption was detected up to a SA concentration of 100 zM against 1 μM BSA. The corresponding selectivity is as high as (SA/BSA) = 1013. It is known that such albumin is included by ~1mM in human blood. Such high concentration completely hampers the detection of low concentration target biomarkers even using our nanolasers. Therefore, our strategy is such that we first dilute the blood plasma to ~1μM, a thousand-fold lower concentration, and then detect the target. Antibodies of target biomarkers typically have affinity constants of 109 – 1011 M−1 order, which are three orders lower than biotin-SA’s. Considering the DL of our nanolaser sensor for biotin-SA, the DL of target biomarkers will be in the sub-fM regime, which is equivalent to sub-pM regime before the dilution. This is a very promising number that enables the detection of various biomarkers of interest for medical diagnoses.

4. Conclusion

Using GaInAsP photonic crystal nanoslot nanolasers modified by biotin, we observed the biotin-SA specific binding for which the detection limit concentration was evaluated from the Langmuir fitting to be 16 zM. We also succeeded in detecting 100 zM SA in the impure sample with 1 μM BSA as the contaminant. This means that the ultra-high selectivity (SA/BSA) = 1013 was achieved. Even when considering different affinities of the biotin-SA binding and actual antibody-antigen binding of biomarkers, this high sensitivity and selectivity will allow simple and fast examination of biomarkers. In addition, the simple fabrication process and measurement of the nanolaser will enable low-cost mass-production, disposable use, easy handling, simple procedure and testing. Thus, our nanolaser will be the promising candidate as a practical biomarker sensor in medical diagnoses.

Acknowledgments

This work was partly supported by the Grant-In-Aid of MEXT, #24226003.

References and links

1.

G.-J. Zhang, Z. H. H. Luo, M. J. Huang, J. J. Ang, T. G. Kang, and H. Ji, “An integrated chip for rapid, sensitive, and multiplexed detection of cardiac biomarkers from fingerprick blood,” Biosens. Bioelectron. 28(1), 459–463 (2011). [CrossRef] [PubMed]

2.

Y. D. Ivanov, V. M. Govorun, V. A. Bykov, and A. I. Archakov, “Nanotechnologies in proteomics,” Proteomics 6(5), 1399–1414 (2006). [CrossRef] [PubMed]

3.

R. Wiese, Y. Belosludtsev, T. Powdrill, P. Thompson, and M. Hogan, “Simultaneous multianalyte ELISA performed on a microarray platform,” Clin. Chem. 47(8), 1451–1457 (2001). [PubMed]

4.

B. J. Luff, J. S. Wilkinson, J. Piehler, U. Hollenbach, J. Ingenhoff, and N. Fabricius, “Integrated optical Mach-Zehnder biosensor,” J. Lightwave Technol. 16(4), 583–592 (1998). [CrossRef]

5.

J. Homola, S. S. Yee, and G. Gauglitz, “Surface plasmon resonance sensors: review,” Sens. Actuators B Chem. 54(1−2), 3–15 (1999). [CrossRef]

6.

W. C. Law, K. T. Yong, A. Baev, R. Hu, and P. N. Prasad, “Nanoparticle enhanced surface plasmon resonance biosensing: application of gold nanorods,” Opt. Express 17(21), 19041–19046 (2009). [CrossRef] [PubMed]

7.

M. Piliarik, M. Bocková, and J. Homola, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Biosens. Bioelectron. 26(4), 1656–1661 (2010). [CrossRef] [PubMed]

8.

A. Yalcin, K. C. Popat, J. C. Aldridge, T. A. Desai, J. Hryniewicz, N. Chbouki, B. E. Little, O. King, V. Van, S. Chu, D. Gill, M. Anthes-Washburn, M. S. Unlu, and B. B. Goldberg, “Optical sensing of biomolecules using microring resonators,” IEEE J. Sel. Top. Quantum Electron. 12(1), 148–155 (2006). [CrossRef]

9.

A. M. Armani, R. P. Kulkarni, S. E. Fraser, R. C. Flagan, and K. J. Vahala, “Label-free, single-molecule detection with optical microcavities,” Science 317(5839), 783–787 (2007). [CrossRef] [PubMed]

10.

F. Vollmer and L. Yang, “Label-free detection with high-Q microcavities: a review of biosensing mechanisms for integrated devices,” Nanophotonics 1(3–4), 267–291 (2012).

11.

M. G. von Muhlen, N. D. Brault, S. M. Knudsen, S. Y. Jiang, and S. R. Manalis, “Label-free biomarker sensing in undiluted serum with suspended microchannel resonators,” Anal. Chem. 82(5), 1905–1910 (2010). [CrossRef] [PubMed]

12.

M. M. A. Hakim, M. Lombardini, K. Sun, F. Giustiniano, P. L. Roach, D. E. Davies, P. H. Howarth, M. R. R. de Planque, H. Morgan, and P. Ashburn, “Thin film polycrystalline silicon nanowire biosensors,” Nano Lett. 12(4), 1868–1872 (2012). [CrossRef] [PubMed]

13.

S. Kita, K. Nozaki, S. Hachuda, H. Watanabe, Y. Saito, S. Otsuka, T. Nakada, Y. Arita, and T. Baba, “Photonic crystal point-shift nanolaser with and without nanoslots −−− design, fabrication, lasing and sensing characteristics,” IEEE J. Sel. Top. Quantum Electron. 17(6), 1632–1647 (2011). [CrossRef]

14.

M. Lončar, A. Scherer, and Y. M. Qiu, “Photonic crystal laser sources for chemical detection,” Appl. Phys. Lett. 82(26), 4648–4650 (2003). [CrossRef]

15.

T. W. Lu, P. T. Lin, K. U. Sio, and P. T. Lee, “Optical sensing of square lattice photonic crystal point-shifted nanocavity for protein adsorption detection,” Appl. Phys. Lett. 96(21), 213702 (2010). [CrossRef]

16.

J. T. Robinson, C. Manolatou, L. Chen, and M. Lipson, “Ultrasmall mode volumes in dielectric optical microcavities,” Phys. Rev. Lett. 95(14), 143901 (2005). [CrossRef] [PubMed]

17.

S. Kita, S. Hachuda, K. Nozaki, and T. Baba, “Nanoslot laser,” Appl. Phys. Lett. 97(16), 161108 (2010). [CrossRef]

18.

S. Kita, S. Hachuda, S. Otsuka, T. Endo, Y. Imai, Y. Nishijima, H. Misawa, and T. Baba, “Super-sensitivity in label-free protein sensing using a nanoslot nanolaser,” Opt. Express 19(18), 17683–17690 (2011). [CrossRef] [PubMed]

19.

M. Narimatsu, S. Kita, H. Abe, and T. Baba, “Enhancement of vertical emission in photonic crystal nanolasers,” Appl. Phys. Lett. 100(12), 121117 (2012). [CrossRef]

20.

K. Watanabe, S. Hachuda, T. Isono, and T. Baba, “Photonic crystal nanolaser sensors with ALD coating”, Conference on Laser & Electro-Opt. Pacific Rim (CLEO) and Optoelectronic & Commun. Conf. / Photonics Switching (2013), paper TuJ2–2.

21.

T. Isono, H. Tanaka, and T. Ogino, ““Effect of chemical modification of the substrate surface on supported lipid bilayer formation,” e-J. Surf. Sci. Nanotech. 5, 99–102 (2007).

22.

N. Nakajima and Y. Ikada, “Mechanism of amide formation by carbodiimide for bioconjugation in aqueous media,” Bioconjug. Chem. 6(1), 123–130 (1995). [CrossRef] [PubMed]

23.

S. Mao, G. H. Lu, K. H. Yu, Z. Bo, and J. H. Chen, “Specific protein detection using thermally reduced graphene oxide sheet decorated with gold nanoparticle-antibody conjugates,” Adv. Mater. 22(32), 3521–3526 (2010). [CrossRef] [PubMed]

24.

K. De Vos, I. Bartolozzi, E. Schacht, P. Bienstman, and R. Baets, “Silicon-on-insulator microring resonator for sensitive and label-free biosensing,” Opt. Express 15(12), 7610–7615 (2007). [CrossRef] [PubMed]

25.

H. Ukeda, T. Ishii, M. Sawamura, and H. Kusunose, “Dynamic analysis of the binding process of bovine serum-albumin on glutaraldehyde-activated controlled-pore glass,” Anal. Chim. Acta 308(1−3), 261–268 (1995). [CrossRef]

OCIS Codes
(170.4580) Medical optics and biotechnology : Optical diagnostics for medicine
(280.1415) Remote sensing and sensors : Biological sensing and sensors
(140.3945) Lasers and laser optics : Microcavities
(230.5298) Optical devices : Photonic crystals

ToC Category:
Medical Optics and Biotechnology

History
Original Manuscript: March 1, 2013
Revised Manuscript: May 13, 2013
Manuscript Accepted: May 14, 2013
Published: May 17, 2013

Virtual Issues
Vol. 8, Iss. 6 Virtual Journal for Biomedical Optics

Citation
Shoji Hachuda, Shota Otsuka, Shota Kita, Toshinari Isono, Michimasa Narimatsu, Keisuke Watanabe, Yoshio Goshima, and Toshihiko Baba, "Selective detection of sub-atto-molar Streptavidin in 1013-fold impure sample using photonic crystal nanolaser sensors," Opt. Express 21, 12815-12821 (2013)
http://www.opticsinfobase.org/vjbo/abstract.cfm?URI=oe-21-10-12815


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References

  1. G.-J. Zhang, Z. H. H. Luo, M. J. Huang, J. J. Ang, T. G. Kang, and H. Ji, “An integrated chip for rapid, sensitive, and multiplexed detection of cardiac biomarkers from fingerprick blood,” Biosens. Bioelectron.28(1), 459–463 (2011). [CrossRef] [PubMed]
  2. Y. D. Ivanov, V. M. Govorun, V. A. Bykov, and A. I. Archakov, “Nanotechnologies in proteomics,” Proteomics6(5), 1399–1414 (2006). [CrossRef] [PubMed]
  3. R. Wiese, Y. Belosludtsev, T. Powdrill, P. Thompson, and M. Hogan, “Simultaneous multianalyte ELISA performed on a microarray platform,” Clin. Chem.47(8), 1451–1457 (2001). [PubMed]
  4. B. J. Luff, J. S. Wilkinson, J. Piehler, U. Hollenbach, J. Ingenhoff, and N. Fabricius, “Integrated optical Mach-Zehnder biosensor,” J. Lightwave Technol.16(4), 583–592 (1998). [CrossRef]
  5. J. Homola, S. S. Yee, and G. Gauglitz, “Surface plasmon resonance sensors: review,” Sens. Actuators B Chem.54(1−2), 3–15 (1999). [CrossRef]
  6. W. C. Law, K. T. Yong, A. Baev, R. Hu, and P. N. Prasad, “Nanoparticle enhanced surface plasmon resonance biosensing: application of gold nanorods,” Opt. Express17(21), 19041–19046 (2009). [CrossRef] [PubMed]
  7. M. Piliarik, M. Bocková, and J. Homola, “Surface plasmon resonance biosensor for parallelized detection of protein biomarkers in diluted blood plasma,” Biosens. Bioelectron.26(4), 1656–1661 (2010). [CrossRef] [PubMed]
  8. A. Yalcin, K. C. Popat, J. C. Aldridge, T. A. Desai, J. Hryniewicz, N. Chbouki, B. E. Little, O. King, V. Van, S. Chu, D. Gill, M. Anthes-Washburn, M. S. Unlu, and B. B. Goldberg, “Optical sensing of biomolecules using microring resonators,” IEEE J. Sel. Top. Quantum Electron.12(1), 148–155 (2006). [CrossRef]
  9. A. M. Armani, R. P. Kulkarni, S. E. Fraser, R. C. Flagan, and K. J. Vahala, “Label-free, single-molecule detection with optical microcavities,” Science317(5839), 783–787 (2007). [CrossRef] [PubMed]
  10. F. Vollmer and L. Yang, “Label-free detection with high-Q microcavities: a review of biosensing mechanisms for integrated devices,” Nanophotonics1(3–4), 267–291 (2012).
  11. M. G. von Muhlen, N. D. Brault, S. M. Knudsen, S. Y. Jiang, and S. R. Manalis, “Label-free biomarker sensing in undiluted serum with suspended microchannel resonators,” Anal. Chem.82(5), 1905–1910 (2010). [CrossRef] [PubMed]
  12. M. M. A. Hakim, M. Lombardini, K. Sun, F. Giustiniano, P. L. Roach, D. E. Davies, P. H. Howarth, M. R. R. de Planque, H. Morgan, and P. Ashburn, “Thin film polycrystalline silicon nanowire biosensors,” Nano Lett.12(4), 1868–1872 (2012). [CrossRef] [PubMed]
  13. S. Kita, K. Nozaki, S. Hachuda, H. Watanabe, Y. Saito, S. Otsuka, T. Nakada, Y. Arita, and T. Baba, “Photonic crystal point-shift nanolaser with and without nanoslots −−− design, fabrication, lasing and sensing characteristics,” IEEE J. Sel. Top. Quantum Electron.17(6), 1632–1647 (2011). [CrossRef]
  14. M. Lončar, A. Scherer, and Y. M. Qiu, “Photonic crystal laser sources for chemical detection,” Appl. Phys. Lett.82(26), 4648–4650 (2003). [CrossRef]
  15. T. W. Lu, P. T. Lin, K. U. Sio, and P. T. Lee, “Optical sensing of square lattice photonic crystal point-shifted nanocavity for protein adsorption detection,” Appl. Phys. Lett.96(21), 213702 (2010). [CrossRef]
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