Abstract

We experimentally demonstrate protein binding at the single particle level. A double nanohole (DNH) optical trap was used to hold onto a 20 nm biotin-coated polystyrene (PS) particle which subsequently is bound to streptavidin. Biotin-streptavidin binding has been detected by an increase in the optical transmission through the DNH. Similar optical transmission behavior was not observed when streptavidin binding sites where blocked by mixing streptavidin with excess biotin. Furthermore, interaction of non-functionalized PS particles with streptavidin did not induce a change in the optical transmission through the DNH. These results are promising as the DNH trap can make an excellent single molecule resolution sensor which would enable studying biomolecular interactions and dynamics at a single particle/molecule level.

©2013 Optical Society of America

1. Introduction

Single protein studies typically bind a protein to a surface and then look at protein-protein interactions through additional binding events [15]. Impressively, recent studies have shown single protein binding sensitivity using plasmonic nanoparticle by monitoring resonance shifts [6] and by photo-thermal transduction to achieve increased sensitivity [7]. Those works, however, have the disadvantage of using one of the binding sites of the protein for the surface-attachment and obscuring/blocking a specific side of the protein by the surface. They also restrict the motion of the protein, and so the binding event is not in its native state.

Optical trapping of single proteins can, in principle, allow for studying protein interactions without the need for surface binding. Recently, our group has developed an optical trapping approach using nano-apertures [8,9], which allows for trapping of single proteins. Here we show single protein binding, using the biotin-streptavidin model system. Since biotin is a small molecule it requires tethering to a larger particle to observe binding with streptavidin, however, we might be able in the future to observe single molecule binding of bigger molecules without the need of tethering because molecules can be held in place by the optical trap. Protein binding is confirmed by performing two appropriate control experiments: 1) we trapped biotin-coated PS particles and then flowed in streptavidin with the binding sites being blocked off by mixing it with excess biotin, and 2) we trapped non-functionalized PS particles and then flowed in streptavidin. Both of the control experiments consistently did not show any binding. We believe that this is the first definitive measurement of single protein binding using an optical trapping system, without the need for tethering the protein to a larger particle.

2. Experimental setup

Figure 1 shows a schematic of the DNH optical trapping system which is based on Thorlabs optical tweezer kit (OTKB). We used an 830 nm continuous laser (Sacher Lasertechnik Group, Model TEC 120) which has the advantage of better detection efficiency for the photodetector than a 980 nm laser and helps with trapping smaller objects due to the favorable wavelength-dependent scaling. The trapping beam was focused into the sample using a 100 × oil immersion microscope objective with a 1.25 numerical aperture. We used an optical density filter (ODF) to limit the optical power at the output of the objective lens. A half-wave plate (HWP) was used to rotate the polarization of the incident beam so that the electric field of the beam is aligned along the cusps of the DNH giving a large local field enhancement and hence creating a strong trapping point.. Transmitted light through the DNH was collected using a 10 × condenser microscope objective with 0.25 numerical aperture, and measured by a silicon-based avalanche photodetector (APD) (Thorlabs APD110A). We used a data acquisition board to record the voltage values generated by the APD at a sampling frequency of 2 kHz. The setup is modified so as to allow for microfluidic delivery to the trapping site where we used a dual Fusion Syringe Pump (Chemyx Inc., Model Fusion 200) to sequentially flow biotin-coated PS particles and streptavidin into the microfluidic channel. Here, we followed the same microfluidic chip fabrication process outlined in the Supporting Information of our previous work on flow dependant trapping [10], with the resultant microfluidic channel dimensions being 65 µm by 800 µm.

 

Fig. 1 A schematic of the DNH optical trap with dual microfluidic input. Abbreviations used: ODF = optical density filter; HWP = half-wave plate; BE = beam expander; MR = mirror; MO = microscope objective; OI MO = oil immersion objective; APD = avalanche photodetector.

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A focused ion beam (Hitachi FB-2100 FIB) was used to mill a DNH in a 100 nm thick Au film on a glass substrate with a 5 nm titanium adhesion layer (EMF Corp.). Figure 2 shows a schematic of the protein binding experiments and ascanning electron microscope image (Hitachi S-4800 FESEM) of the DNH used in trapping experiments. The separation between the cusps was measured to be 30 nm which is close to the optimal 25 nm separation found to be the best for trapping 20 nm PS particles according to our previous studies [11]. As with our previous work on trapping a protein, prior to conducting trapping experiments we formed a monolayer of mPEG thiol on the Au surface by immersing the Au sample in a 5 mM aqueous solution of mPEG thiol (molecular weight, 5 kDa) at room temperature overnight and then rinsing it with DI water. This helps prevent streptavidin from adsorbing on the Au surface.

 

Fig. 2 A schematic showing the protein binding experiments .(a) 20 nm biotin-coated PS particle approaches the DNH. (b) Introduction of streptavidin to the trapping site once a successful trapping event of 20 nm biotin-coated PS particle is achieved. (c) Streptavidin is bound to biotin between the two sharp cusps of the DNH. (d) A scanning electron microscope image of the DNH used in the protein binding and control experiments.

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Here we experimentally demonstrate protein binding by trapping 20 nm biotin-coated PS particles (NANOCS PS20-BN-2) and then bind it with streptavidin with a molecular weight 60 kDa. The streptavidin was purchased in powder form (SIGMA-ALDRICH, Product No. 85878) and the desired concentration was obtained by dissolving it in phosphate buffered saline (PBS). Biotin, which is also known as vitamin B7 and vitamin H, has an extraordinary binding affinity to streptavidin, with a dissociation constant in the order of about 10−14 mol/L, making it the strongest non covalent bond found in nature [12].

3. Protein binding experiments

3.1 Protein binding detection

Figure 3 shows the time evolution of the optical power transmitted through the DNH and the schematics the corresponding steps of the protein binding experiments, where (a) shows flowing 20 nm biotin-coated PS particles (0.01% w/v in DI water), (b) trapping event of 20 nm biotin-coated PS particle between the two sharp tips of the DNH and subsequently flowing streptavidin (0.01% w/v in PBS), (c) binding of streptavidin with the trapped biotin-coated PS particle. We repeated all of the experiments and controls at least 4 times. When a biotin-coated PS particle gets trapped between the cusps of the DNH it dielectrically loads the region and causes an enhancement of the local optical field intensity and increased DNH transmission [1318]. Once a stable trapping event of a biotin-coated PS particle is achieved, streptavidin is flowed into the channel where it gets bound to the trapped particle, causing further dielectric loading to the DNH region and consequently a higher optical transmission is obtained. We used a moderate flow rate of 5 µL/min which enables fast enough delivery of streptavidin to the trapping site and at the same time does not wash away the trapped particle, as was investigated in one of our previous studies [10].

 

Fig. 3 Time trace of optical transmission through the DNH where (a) shows flowing 20 nm biotin-coated PS particles through the microfluidic channel, (b) trapping of 20 nm biotin-coated PS particle between the two sharp tips formed by two overlapping DNHs and subsequently flowing streptavidin, and (c) binding between 20 nm biotin-coated PS particle and streptavidin.

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The setup is designed such that delivery of streptavidin to the trapping site takes about 150 seconds from the time a successful trapping of biotin-coated PS particle is achieved. The delivery time of streptavidin to the trapping site of 150 seconds was related to the time for it to flow from the syringe to the trapping site at a flow rate of 5 µL/min. This indicates that a binding event occurs within a few seconds after the introduction of streptavidin to the trapping site, which is expected due to the high binding affinity of the streptavidin-biotin pair. Similar binding results were obtained on different days and with freshly made solutions. After each set of experiments, we flowed deionized water through the microfluidic channel for 30 minutes to make sure that the channel is clean for the next set of experiments.

4. Control experiments

To show clearly that we are actually observing specific streptavidin-biotin binding, and not just co-trapping, we performed two separate control experiments using: 1) saturated streptavidin, 2) non-functionalized PS particles.

4.1 Saturated streptavidin

Figure 4 shows the time trace of the optical transmission through the DNH with the schematic of the corresponding steps for the saturated streptavidin control experiment where, (a) shows flowing 20 nm biotin-coated PS particles, (b) trapping event of 20 nm biotin-coated PS particle and subsequently flowing saturated streptavidin, and (c) saturated streptavidin does not bind to the trapped 20 nm biotin-coated PS particle. In this set of control experiments, we trapped a biotin-coated PS particle and then flowed in saturated streptavidin in which all the binding sites were blocked off by mixing it with excess biotin (SIGMA-ALDRICH), molecular weight 344.31 Da. As the figure shows, there is an increase in the optical transmission through the DNH observed after flowing the 20 nm biotin-coated PS particles indicating a successful trapping event of biotin-coated PS particle. However, we have not observed any further increase in the optical transmission for the subsequent 25 minutes after flowing saturated streptavidin.

 

Fig. 4 Time trace of optical transmission through the DNH for the saturated streptavidin control experiment where (a) shows flowing 20 nm biotin-coated PS particles through the microfluidic channel, (b) trapping of 20 nm biotin-coated PS particle between the cusps of the DNH and subsequently flowing saturated streptavidin, and (c) saturated streptavidin does not bind to the trapped 20 nm biotin-coated PS particle.

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4.2 Non-functionalized PS particles

Figure 5 shows the time evolution of optical transmission through the DNH with the schematic of the corresponding steps for the non-functionalized 20 nm PS particles where (a) shows flowing 20 nm non-functionalized PS particles (0.01% in DI water), (b) trapping event of 20 nm PS particle and then flowing streptavidin, and (c) streptavidin does not bind to the trapped 20 nm PS particle. Here, we flowed in streptavidin (with the same concentration used in the main binding experiments) after successfully achieving a trapping event of a 20 nm non-functionalized PS particle. Introduction of streptavidin to the trapping site did not cause any change in the optical transmission through the DNH for the subsequent 25 minutes after achieving a stable trapping event of a non-functionalized PS particle.

 

Fig. 5 Time trace of optical transmission through the DNH for the non-functionalized PS particle control experiment where (a) shows flowing 20 nm PS particles through the microfluidic channel, (b) trapping of 20 nm PS particle between the cusps of the DNH and subsequently flowing streptavidin, and (c) streptavidin does not bind to the trapped 20 nm PS particle.

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5. Discussion

5.1 DNH trap for single protein binding detection

Our objective in this current study has been to observe single protein binding using the DNH trap system. Our experimental results on single protein binding as well as the control experiments explicitly demonstrate that single protein binding detection is achievable by using the DNH optical trap system. Unlike other detection systems which require tethering and/or surface functionalizeation of the particles of interest [1924], our system uses the trapping laser beam to hold the trapped particle in a well defined trapping region between the two cusps of the DNH. Furthermore, our DNH trap allows for single protein binding detection by simply measuring optical transmission of the same trapping laser beam through the DNH aperture without the need of measuring wavelength or having additional laser sources [2528] or fluorescently labeling the target particle [29]. This straightforward intensity measurement of optical transmission could yield a much faster detection of protein binding and therefore, allow the study of single protein binding dynamics at a nanosecond scale. Besides, the distinct and abrupt jump in the optical transmission through the DNH serves as a potential protein binding sensor with a signal-to-noise ratio (SNR) of 18. Indeed a recent study used a streptavidin–R-phycoerythrin conjugate with a molecular weight of 300 kDa (50 times bigger molecule than the one we used in our study) to clearly detect protein binding using surface plasmon resonance shift of Au nanorods [7].

Protein-protein interactions are generally temperature-sensitive and require systems which operate below the denaturation temperature of the proteins under study. For instance, recent works on protein studies, like the resonant-based plasmonic particle trapping [3032] and photonic crystal trapping [33,34] systems suffer from heating effects and might need to apply one or more thermal management strategies to overcome heating issues; for example, the use of adjacent metal films as a natural heat sink in nanopillar plasmonic trapping [35,36]. These resonant trapping systems do not only generate heat under resonant absorption but also add experimental complexity in terms of applying thermal management strategies. On the other hand, the DNH trap system is non-resonant and the Au film plays a role in reducing the heating effects due to its good thermal conductivity. Considering other works on optical trapping where there is a metal membrane [36], we expect that the temperature increase is only a few degrees celcius and so this is not expected to hinder protein binding, protein folding, or other molecular investigations. We are presently working on integrating Raman into the setup so that we could potentially measure the temperature distribution by looking at the ratio between Stokes and anti-Stokes peaks. Here, we expect the temperature at the trapping point to be well below 70 °C as this is the temperature required to break the streptavidin-biotin bond without denaturing streptavidin [37] and such thermal effects on streptavidin-biotin pair have not been observed in our experiments. This feature makes our DNH optical aperture trapping system thermally suitable for protein-protein studies, for example, studying the dynamics of protein folding and unfolding of BSA [8].

It is possible to envision schemes whereby the optical polarization may be used to rotate the trapped molecules, as has been achieved for other works [38]. The double nanohole constrains the polarization of the maximum trapping field along the cusps between the two nanoholes, and therefore rotation is not possible.

In our previous studies we found that steric hindrance prevents co-trapping of two similar particles in the region between the two sharp tips of DNH [10]. Therefore, it stands reasonable here to assume that co-trapping of two 20 nm biotin-coated PS particles in a 30 nm gap is subject to steric hindrance too. Indeed, in our current study we have neither observed co-trapping of a biotin-coated PS particle with another biotin-coated PS particle nor co-trapping of streptavidin with streptavidin. In addition, we have not observed any co-trapping behavior in our control experiments. This further proves that the results obtained in this study are as a consequence of streptavidin-biotin binding and not co-trapping of two similar particles.

5.2 Future directions

It is interesting that we observed protein binding at a single molecule level using the DNH aperture trap. We aim to extend our study to further test the binding sensitivity of our system by using binding affinity pairs which have lower disassociation constants. In addition, there is also the potential of analyzing time traces of binding events of different binding affinity pairs to investigate the possibility of identifying the nature of trapped/bound particle(s). It is also possible to modify our existing setup to analyze the Raman signal of the trapped/bound particle(s) for which we have experience with Raman spectroscopy [39]. We are presently attempting to simultaneously measure the Raman signal of the trapped object by using the trapping laser as the Raman excitation source, as well as appropriate filters and a spectrometer after the double nanohole. Moreover, it is interesting to study isolated nanoparticles within a heterogeneous mixture. Furthermore, we are interested in studying the dynamics of folding and unfolding of single proteins. Moreover, we are interested in fluorescence studies of trapped particles provided that quenching effects at the Au surface can be avoided.

6. Conclusion

In conclusion, we have used a DNH-based optical trap to detect streptavidin-biotin binding at the single molecule level. This was achieved by measuring the optical transmission through the DNH. To further confirm that the observed increase in optical transmission through the DNH is due to the specific binding of streptavidin to biotin, we preformed two appropriate control experiments that did not show binding, i.e. using saturated streptavidin and non-functionalized PS particles. The control experiment results were consistent with the main experimental results. These results are promising for biomolecular interaction studies at the single molecule/particle level; for example studying single protein binding interactions and dynamics at single molecule level.

Acknowledgment

The authors acknowledge support from the Natural Sciences and Engineering Research Council (Canada) Discovery Grant Program.

References and links

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References

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  1. J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
    [Crossref] [PubMed]
  2. A. Abbas, M. J. Linman, and Q. A. Cheng, “New trends in instrumental design for surface plasmon resonance-based biosensors,” Biosens. Bioelectron. 26(5), 1815–1824 (2011).
    [Crossref] [PubMed]
  3. C. Cecconi, E. A. Shank, C. Bustamante, and S. Marqusee, “Direct Observation of the Three-State Folding of a Single Protein Molecule,” Science 309(5743), 2057–2060 (2005).
    [Crossref] [PubMed]
  4. A. Hoffmann, K. Neupane, and M. T. Woodside, “Single-molecule assays for investigating protein misfolding and aggregation,” Phys. Chem. Chem. Phys. 15(21), 7934–7948 (2013).
    [Crossref] [PubMed]
  5. A. Borgia, P. M. Williams, and J. Clarke, “Single-Molecule Studies of Protein Folding,” Annu. Rev. Biochem. 77(1), 101–125 (2008).
    [Crossref] [PubMed]
  6. I. Ament, J. Prasad, A. Henkel, S. Schmachtel, and C. Sönnichsen, “Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles,” Nano Lett. 12(2), 1092–1095 (2012).
    [Crossref] [PubMed]
  7. P. Zijlstra, P. M. R. Paulo, and M. Orrit, “Optical detection of single non-absorbing molecules using the surface plasmon resonance of a gold nanorod,” Nat. Nanotechnol. 7(6), 379–382 (2012).
    [Crossref] [PubMed]
  8. Y. Pang and R. Gordon, “Optical Trapping of a Single Protein,” Nano Lett. 12(1), 402–406 (2012).
    [Crossref] [PubMed]
  9. A. Zehtabi-Oskuie, H. Jiang, B. R. Cyr, D. W. Rennehan, A. A. Al-Balushi, and R. Gordon, “Double nanohole optical trapping: dynamics and protein-antibody co-trapping,” Lab Chip 13(13), 2563–2568 (2013).
    [Crossref] [PubMed]
  10. A. Zehtabi-Oskuie, J. G. Bergeron, and R. Gordon, “Flow-dependent double-nanohole optical trapping of 20 nm polystyrene nanospheres,” Sci Rep 2, 966 (2012).
    [Crossref] [PubMed]
  11. Y. Pang and R. Gordon, “Optical Trapping of 12 nm Dielectric Spheres Using Double-Nanoholes in a Gold Film,” Nano Lett. 11(9), 3763–3767 (2011).
    [Crossref] [PubMed]
  12. N. M. Green, “Avidin,” Adv. Protein Chem. 29, 85–133 (1975).
    [Crossref] [PubMed]
  13. L. Huang and O. J. F. Martin, “Reversal of the optical force in a plasmonic trap,” Opt. Lett. 33(24), 3001–3003 (2008).
    [Crossref] [PubMed]
  14. M. Nieto-Vesperinas, P. C. Chaumet, and A. Rahmani, “Near-field photonic forces,” Philos Trans A Math Phys Eng Sci 362(1817), 719–737 (2004).
    [Crossref] [PubMed]
  15. K. Okamoto and S. Kawata, “Radiation force exerted on subwavelength particles near a nanoaperture,” Phys. Rev. Lett. 83(22), 4534–4537 (1999).
    [Crossref]
  16. L. Novotny, R. X. Bian, and X. S. Xie, “Theory of nanometric optical tweezers,” Phys. Rev. Lett. 79(4), 645–648 (1997).
    [Crossref]
  17. M. Juan, R. Gordon, Y. Pang, F. Eftekhari, and R. Quidant, “Self-induced back-action optical trapping of dielectric nanoparticles,” Nat. Phys. 5(12), 915–919 (2009).
    [Crossref]
  18. M. L. Juan, M. Righini, and R. Quidant, “Plasmon nano-optical tweezers,” Nat. Photonics 5(6), 349–356 (2011).
    [Crossref]
  19. Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire Nanosensors for Highly Sensitive and Selective Detection of Biological and Chemical Species,” Science 293(5533), 1289–1292 (2001).
    [Crossref] [PubMed]
  20. M. D. Wang, H. Yin, R. Landick, J. Gelles, and S. M. Block, “Stretching DNA with Optical Tweezers,” Biophys. J. 72(3), 1335–1346 (1997).
    [Crossref] [PubMed]
  21. E. A. Abbondanzieri, W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. M. Block, “Direct observation of base-pair stepping by RNA polymerase,” Nature 438(7067), 460–465 (2005).
    [Crossref] [PubMed]
  22. J. T. Finer, R. M. Simmons, and J. A. Spudich, “Single myosin molecule mechanics: piconewton forces and nanometre steps,” Nature 368(6467), 113–119 (1994).
    [Crossref] [PubMed]
  23. Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
    [Crossref] [PubMed]
  24. J. Nilsson, M. Evander, B. Hammarström, and T. Laurell, “Review of cell and particle trapping in microfluidic systems,” Anal. Chim. Acta 649(2), 141–157 (2009).
    [Crossref] [PubMed]
  25. H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
    [Crossref]
  26. M. J. Lang, C. L. Asbury, J. W. Shaevitz, and S. M. Block, “An Automated Two-Dimensional Optical Force Clamp for Single Molecule Studies,” Biophys. J. 83(1), 491–501 (2002).
    [Crossref] [PubMed]
  27. W. J. Greenleaf, M. T. Woodside, E. A. Abbondanzieri, and S. M. Block, “Passive All-Optical Force Clamp for High-Resolution Laser Trapping,” Phys. Rev. Lett. 95(20), 208102 (2005).
    [Crossref] [PubMed]
  28. K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Scannable Plasmonic Trapping Using a Gold Stripe,” Nano Lett. 10(9), 3506–3511 (2010).
    [Crossref] [PubMed]
  29. A. P. Fields and A. E. Cohen, “Electrokinetic trapping at the one nanometer limit,” Proc. Natl. Acad. Sci. U.S.A. 108(22), 8937–8942 (2011).
    [Crossref] [PubMed]
  30. J. S. Donner, G. Baffou, D. McCloskey, and R. Quidant, “Plasmon-Assisted Optofluidics,” ACS Nano 5(7), 5457–5462 (2011).
    [Crossref] [PubMed]
  31. N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).
  32. A. A. E. Saleh and J. A. Dionne, “Toward Efficient Optical Trapping of Sub-10-nm Particles with Coaxial Plasmonic Apertures,” Nano Lett. 12(11), 5581–5586 (2012).
    [Crossref] [PubMed]
  33. Y. F. Chen, X. Serey, R. Sarkar, P. Chen, and D. Erickson, “Controlled Photonic Manipulation of Proteins and Other Nanomaterials,” Nano Lett. 12(3), 1633–1637 (2012).
    [Crossref] [PubMed]
  34. S. Lin and K. B. Crozier, “Trapping-Assisted Sensing of Particles and Proteins Using On-Chip Optical Microcavities,” ACS Nano 7(2), 1725–1730 (2013).
    [Crossref] [PubMed]
  35. K. Wang and K. B. Crozier, “Plasmonic Trapping with a Gold Nanopillar,” ChemPhysChem 13(11), 2639–2648 (2012).
    [Crossref] [PubMed]
  36. K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Trapping and rotating nanoparticles using a plasmonic nano-tweezer with an integrated heat sink,” Nat Commun 2, 469 (2011).
    [Crossref] [PubMed]
  37. A. Holmberg, A. Blomstergren, O. Nord, M. Lukacs, J. Lundeberg, and M. Uhlén, “The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures,” Electrophoresis 26(3), 501–510 (2005).
    [Crossref] [PubMed]
  38. M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
    [Crossref] [PubMed]
  39. A. Ahmed and R. Gordon, “Directivity Enhanced Raman Spectroscopy using Nanoantennas,” Nano Lett. 11(4), 1800–1803 (2011).
    [Crossref] [PubMed]

2013 (5)

A. Hoffmann, K. Neupane, and M. T. Woodside, “Single-molecule assays for investigating protein misfolding and aggregation,” Phys. Chem. Chem. Phys. 15(21), 7934–7948 (2013).
[Crossref] [PubMed]

A. Zehtabi-Oskuie, H. Jiang, B. R. Cyr, D. W. Rennehan, A. A. Al-Balushi, and R. Gordon, “Double nanohole optical trapping: dynamics and protein-antibody co-trapping,” Lab Chip 13(13), 2563–2568 (2013).
[Crossref] [PubMed]

N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).

S. Lin and K. B. Crozier, “Trapping-Assisted Sensing of Particles and Proteins Using On-Chip Optical Microcavities,” ACS Nano 7(2), 1725–1730 (2013).
[Crossref] [PubMed]

M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
[Crossref] [PubMed]

2012 (7)

K. Wang and K. B. Crozier, “Plasmonic Trapping with a Gold Nanopillar,” ChemPhysChem 13(11), 2639–2648 (2012).
[Crossref] [PubMed]

A. A. E. Saleh and J. A. Dionne, “Toward Efficient Optical Trapping of Sub-10-nm Particles with Coaxial Plasmonic Apertures,” Nano Lett. 12(11), 5581–5586 (2012).
[Crossref] [PubMed]

Y. F. Chen, X. Serey, R. Sarkar, P. Chen, and D. Erickson, “Controlled Photonic Manipulation of Proteins and Other Nanomaterials,” Nano Lett. 12(3), 1633–1637 (2012).
[Crossref] [PubMed]

A. Zehtabi-Oskuie, J. G. Bergeron, and R. Gordon, “Flow-dependent double-nanohole optical trapping of 20 nm polystyrene nanospheres,” Sci Rep 2, 966 (2012).
[Crossref] [PubMed]

I. Ament, J. Prasad, A. Henkel, S. Schmachtel, and C. Sönnichsen, “Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles,” Nano Lett. 12(2), 1092–1095 (2012).
[Crossref] [PubMed]

P. Zijlstra, P. M. R. Paulo, and M. Orrit, “Optical detection of single non-absorbing molecules using the surface plasmon resonance of a gold nanorod,” Nat. Nanotechnol. 7(6), 379–382 (2012).
[Crossref] [PubMed]

Y. Pang and R. Gordon, “Optical Trapping of a Single Protein,” Nano Lett. 12(1), 402–406 (2012).
[Crossref] [PubMed]

2011 (9)

M. L. Juan, M. Righini, and R. Quidant, “Plasmon nano-optical tweezers,” Nat. Photonics 5(6), 349–356 (2011).
[Crossref]

Y. Pang and R. Gordon, “Optical Trapping of 12 nm Dielectric Spheres Using Double-Nanoholes in a Gold Film,” Nano Lett. 11(9), 3763–3767 (2011).
[Crossref] [PubMed]

J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
[Crossref] [PubMed]

A. Abbas, M. J. Linman, and Q. A. Cheng, “New trends in instrumental design for surface plasmon resonance-based biosensors,” Biosens. Bioelectron. 26(5), 1815–1824 (2011).
[Crossref] [PubMed]

A. P. Fields and A. E. Cohen, “Electrokinetic trapping at the one nanometer limit,” Proc. Natl. Acad. Sci. U.S.A. 108(22), 8937–8942 (2011).
[Crossref] [PubMed]

J. S. Donner, G. Baffou, D. McCloskey, and R. Quidant, “Plasmon-Assisted Optofluidics,” ACS Nano 5(7), 5457–5462 (2011).
[Crossref] [PubMed]

K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Trapping and rotating nanoparticles using a plasmonic nano-tweezer with an integrated heat sink,” Nat Commun 2, 469 (2011).
[Crossref] [PubMed]

Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
[Crossref] [PubMed]

A. Ahmed and R. Gordon, “Directivity Enhanced Raman Spectroscopy using Nanoantennas,” Nano Lett. 11(4), 1800–1803 (2011).
[Crossref] [PubMed]

2010 (1)

K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Scannable Plasmonic Trapping Using a Gold Stripe,” Nano Lett. 10(9), 3506–3511 (2010).
[Crossref] [PubMed]

2009 (2)

J. Nilsson, M. Evander, B. Hammarström, and T. Laurell, “Review of cell and particle trapping in microfluidic systems,” Anal. Chim. Acta 649(2), 141–157 (2009).
[Crossref] [PubMed]

M. Juan, R. Gordon, Y. Pang, F. Eftekhari, and R. Quidant, “Self-induced back-action optical trapping of dielectric nanoparticles,” Nat. Phys. 5(12), 915–919 (2009).
[Crossref]

2008 (2)

A. Borgia, P. M. Williams, and J. Clarke, “Single-Molecule Studies of Protein Folding,” Annu. Rev. Biochem. 77(1), 101–125 (2008).
[Crossref] [PubMed]

L. Huang and O. J. F. Martin, “Reversal of the optical force in a plasmonic trap,” Opt. Lett. 33(24), 3001–3003 (2008).
[Crossref] [PubMed]

2006 (1)

H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
[Crossref]

2005 (4)

W. J. Greenleaf, M. T. Woodside, E. A. Abbondanzieri, and S. M. Block, “Passive All-Optical Force Clamp for High-Resolution Laser Trapping,” Phys. Rev. Lett. 95(20), 208102 (2005).
[Crossref] [PubMed]

E. A. Abbondanzieri, W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. M. Block, “Direct observation of base-pair stepping by RNA polymerase,” Nature 438(7067), 460–465 (2005).
[Crossref] [PubMed]

A. Holmberg, A. Blomstergren, O. Nord, M. Lukacs, J. Lundeberg, and M. Uhlén, “The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures,” Electrophoresis 26(3), 501–510 (2005).
[Crossref] [PubMed]

C. Cecconi, E. A. Shank, C. Bustamante, and S. Marqusee, “Direct Observation of the Three-State Folding of a Single Protein Molecule,” Science 309(5743), 2057–2060 (2005).
[Crossref] [PubMed]

2004 (1)

M. Nieto-Vesperinas, P. C. Chaumet, and A. Rahmani, “Near-field photonic forces,” Philos Trans A Math Phys Eng Sci 362(1817), 719–737 (2004).
[Crossref] [PubMed]

2002 (1)

M. J. Lang, C. L. Asbury, J. W. Shaevitz, and S. M. Block, “An Automated Two-Dimensional Optical Force Clamp for Single Molecule Studies,” Biophys. J. 83(1), 491–501 (2002).
[Crossref] [PubMed]

2001 (1)

Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire Nanosensors for Highly Sensitive and Selective Detection of Biological and Chemical Species,” Science 293(5533), 1289–1292 (2001).
[Crossref] [PubMed]

1999 (1)

K. Okamoto and S. Kawata, “Radiation force exerted on subwavelength particles near a nanoaperture,” Phys. Rev. Lett. 83(22), 4534–4537 (1999).
[Crossref]

1997 (2)

L. Novotny, R. X. Bian, and X. S. Xie, “Theory of nanometric optical tweezers,” Phys. Rev. Lett. 79(4), 645–648 (1997).
[Crossref]

M. D. Wang, H. Yin, R. Landick, J. Gelles, and S. M. Block, “Stretching DNA with Optical Tweezers,” Biophys. J. 72(3), 1335–1346 (1997).
[Crossref] [PubMed]

1994 (1)

J. T. Finer, R. M. Simmons, and J. A. Spudich, “Single myosin molecule mechanics: piconewton forces and nanometre steps,” Nature 368(6467), 113–119 (1994).
[Crossref] [PubMed]

1975 (1)

N. M. Green, “Avidin,” Adv. Protein Chem. 29, 85–133 (1975).
[Crossref] [PubMed]

Abbas, A.

A. Abbas, M. J. Linman, and Q. A. Cheng, “New trends in instrumental design for surface plasmon resonance-based biosensors,” Biosens. Bioelectron. 26(5), 1815–1824 (2011).
[Crossref] [PubMed]

Abbondanzieri, E. A.

E. A. Abbondanzieri, W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. M. Block, “Direct observation of base-pair stepping by RNA polymerase,” Nature 438(7067), 460–465 (2005).
[Crossref] [PubMed]

W. J. Greenleaf, M. T. Woodside, E. A. Abbondanzieri, and S. M. Block, “Passive All-Optical Force Clamp for High-Resolution Laser Trapping,” Phys. Rev. Lett. 95(20), 208102 (2005).
[Crossref] [PubMed]

Ahmed, A.

A. Ahmed and R. Gordon, “Directivity Enhanced Raman Spectroscopy using Nanoantennas,” Nano Lett. 11(4), 1800–1803 (2011).
[Crossref] [PubMed]

Ahn, J. H.

J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
[Crossref] [PubMed]

Al-Balushi, A. A.

A. Zehtabi-Oskuie, H. Jiang, B. R. Cyr, D. W. Rennehan, A. A. Al-Balushi, and R. Gordon, “Double nanohole optical trapping: dynamics and protein-antibody co-trapping,” Lab Chip 13(13), 2563–2568 (2013).
[Crossref] [PubMed]

Albert, J.

Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
[Crossref] [PubMed]

Ament, I.

I. Ament, J. Prasad, A. Henkel, S. Schmachtel, and C. Sönnichsen, “Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles,” Nano Lett. 12(2), 1092–1095 (2012).
[Crossref] [PubMed]

Asbury, C. L.

M. J. Lang, C. L. Asbury, J. W. Shaevitz, and S. M. Block, “An Automated Two-Dimensional Optical Force Clamp for Single Molecule Studies,” Biophys. J. 83(1), 491–501 (2002).
[Crossref] [PubMed]

Baffou, G.

J. S. Donner, G. Baffou, D. McCloskey, and R. Quidant, “Plasmon-Assisted Optofluidics,” ACS Nano 5(7), 5457–5462 (2011).
[Crossref] [PubMed]

Barone, P. W.

J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
[Crossref] [PubMed]

Bergeron, J. G.

A. Zehtabi-Oskuie, J. G. Bergeron, and R. Gordon, “Flow-dependent double-nanohole optical trapping of 20 nm polystyrene nanospheres,” Sci Rep 2, 966 (2012).
[Crossref] [PubMed]

Bian, R. X.

L. Novotny, R. X. Bian, and X. S. Xie, “Theory of nanometric optical tweezers,” Phys. Rev. Lett. 79(4), 645–648 (1997).
[Crossref]

Blair, D. A. D.

Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
[Crossref] [PubMed]

Block, S. M.

E. A. Abbondanzieri, W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. M. Block, “Direct observation of base-pair stepping by RNA polymerase,” Nature 438(7067), 460–465 (2005).
[Crossref] [PubMed]

W. J. Greenleaf, M. T. Woodside, E. A. Abbondanzieri, and S. M. Block, “Passive All-Optical Force Clamp for High-Resolution Laser Trapping,” Phys. Rev. Lett. 95(20), 208102 (2005).
[Crossref] [PubMed]

M. J. Lang, C. L. Asbury, J. W. Shaevitz, and S. M. Block, “An Automated Two-Dimensional Optical Force Clamp for Single Molecule Studies,” Biophys. J. 83(1), 491–501 (2002).
[Crossref] [PubMed]

M. D. Wang, H. Yin, R. Landick, J. Gelles, and S. M. Block, “Stretching DNA with Optical Tweezers,” Biophys. J. 72(3), 1335–1346 (1997).
[Crossref] [PubMed]

Blomstergren, A.

A. Holmberg, A. Blomstergren, O. Nord, M. Lukacs, J. Lundeberg, and M. Uhlén, “The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures,” Electrophoresis 26(3), 501–510 (2005).
[Crossref] [PubMed]

Boghossian, A. A.

J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
[Crossref] [PubMed]

Borgia, A.

A. Borgia, P. M. Williams, and J. Clarke, “Single-Molecule Studies of Protein Folding,” Annu. Rev. Biochem. 77(1), 101–125 (2008).
[Crossref] [PubMed]

Brown, L. J.

M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
[Crossref] [PubMed]

Bustamante, C.

C. Cecconi, E. A. Shank, C. Bustamante, and S. Marqusee, “Direct Observation of the Three-State Folding of a Single Protein Molecule,” Science 309(5743), 2057–2060 (2005).
[Crossref] [PubMed]

Cecconi, C.

C. Cecconi, E. A. Shank, C. Bustamante, and S. Marqusee, “Direct Observation of the Three-State Folding of a Single Protein Molecule,” Science 309(5743), 2057–2060 (2005).
[Crossref] [PubMed]

Chang, A. C.

J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
[Crossref] [PubMed]

Chaumet, P. C.

M. Nieto-Vesperinas, P. C. Chaumet, and A. Rahmani, “Near-field photonic forces,” Philos Trans A Math Phys Eng Sci 362(1817), 719–737 (2004).
[Crossref] [PubMed]

Chen, P.

Y. F. Chen, X. Serey, R. Sarkar, P. Chen, and D. Erickson, “Controlled Photonic Manipulation of Proteins and Other Nanomaterials,” Nano Lett. 12(3), 1633–1637 (2012).
[Crossref] [PubMed]

Chen, X.

N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).

Chen, Y. F.

Y. F. Chen, X. Serey, R. Sarkar, P. Chen, and D. Erickson, “Controlled Photonic Manipulation of Proteins and Other Nanomaterials,” Nano Lett. 12(3), 1633–1637 (2012).
[Crossref] [PubMed]

Cheng, Q. A.

A. Abbas, M. J. Linman, and Q. A. Cheng, “New trends in instrumental design for surface plasmon resonance-based biosensors,” Biosens. Bioelectron. 26(5), 1815–1824 (2011).
[Crossref] [PubMed]

Cherukulappurath, S.

N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).

Clarke, J.

A. Borgia, P. M. Williams, and J. Clarke, “Single-Molecule Studies of Protein Folding,” Annu. Rev. Biochem. 77(1), 101–125 (2008).
[Crossref] [PubMed]

Cohen, A. E.

A. P. Fields and A. E. Cohen, “Electrokinetic trapping at the one nanometer limit,” Proc. Natl. Acad. Sci. U.S.A. 108(22), 8937–8942 (2011).
[Crossref] [PubMed]

Crozier, K. B.

S. Lin and K. B. Crozier, “Trapping-Assisted Sensing of Particles and Proteins Using On-Chip Optical Microcavities,” ACS Nano 7(2), 1725–1730 (2013).
[Crossref] [PubMed]

K. Wang and K. B. Crozier, “Plasmonic Trapping with a Gold Nanopillar,” ChemPhysChem 13(11), 2639–2648 (2012).
[Crossref] [PubMed]

K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Trapping and rotating nanoparticles using a plasmonic nano-tweezer with an integrated heat sink,” Nat Commun 2, 469 (2011).
[Crossref] [PubMed]

K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Scannable Plasmonic Trapping Using a Gold Stripe,” Nano Lett. 10(9), 3506–3511 (2010).
[Crossref] [PubMed]

Cui, Y.

Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire Nanosensors for Highly Sensitive and Selective Detection of Biological and Chemical Species,” Science 293(5533), 1289–1292 (2001).
[Crossref] [PubMed]

Cyr, B. R.

A. Zehtabi-Oskuie, H. Jiang, B. R. Cyr, D. W. Rennehan, A. A. Al-Balushi, and R. Gordon, “Double nanohole optical trapping: dynamics and protein-antibody co-trapping,” Lab Chip 13(13), 2563–2568 (2013).
[Crossref] [PubMed]

de Abajo, F. J.

M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
[Crossref] [PubMed]

DeRosa, M. C.

Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
[Crossref] [PubMed]

Dionne, J. A.

A. A. E. Saleh and J. A. Dionne, “Toward Efficient Optical Trapping of Sub-10-nm Particles with Coaxial Plasmonic Apertures,” Nano Lett. 12(11), 5581–5586 (2012).
[Crossref] [PubMed]

Donner, J. S.

J. S. Donner, G. Baffou, D. McCloskey, and R. Quidant, “Plasmon-Assisted Optofluidics,” ACS Nano 5(7), 5457–5462 (2011).
[Crossref] [PubMed]

Eftekhari, F.

M. Juan, R. Gordon, Y. Pang, F. Eftekhari, and R. Quidant, “Self-induced back-action optical trapping of dielectric nanoparticles,” Nat. Phys. 5(12), 915–919 (2009).
[Crossref]

Erickson, D.

Y. F. Chen, X. Serey, R. Sarkar, P. Chen, and D. Erickson, “Controlled Photonic Manipulation of Proteins and Other Nanomaterials,” Nano Lett. 12(3), 1633–1637 (2012).
[Crossref] [PubMed]

Evander, M.

J. Nilsson, M. Evander, B. Hammarström, and T. Laurell, “Review of cell and particle trapping in microfluidic systems,” Anal. Chim. Acta 649(2), 141–157 (2009).
[Crossref] [PubMed]

Fields, A. P.

A. P. Fields and A. E. Cohen, “Electrokinetic trapping at the one nanometer limit,” Proc. Natl. Acad. Sci. U.S.A. 108(22), 8937–8942 (2011).
[Crossref] [PubMed]

Finer, J. T.

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N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).

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H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
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M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
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H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
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E. A. Abbondanzieri, W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. M. Block, “Direct observation of base-pair stepping by RNA polymerase,” Nature 438(7067), 460–465 (2005).
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M. D. Wang, H. Yin, R. Landick, J. Gelles, and S. M. Block, “Stretching DNA with Optical Tweezers,” Biophys. J. 72(3), 1335–1346 (1997).
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M. J. Lang, C. L. Asbury, J. W. Shaevitz, and S. M. Block, “An Automated Two-Dimensional Optical Force Clamp for Single Molecule Studies,” Biophys. J. 83(1), 491–501 (2002).
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J. Nilsson, M. Evander, B. Hammarström, and T. Laurell, “Review of cell and particle trapping in microfluidic systems,” Anal. Chim. Acta 649(2), 141–157 (2009).
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Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire Nanosensors for Highly Sensitive and Selective Detection of Biological and Chemical Species,” Science 293(5533), 1289–1292 (2001).
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N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).

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A. Holmberg, A. Blomstergren, O. Nord, M. Lukacs, J. Lundeberg, and M. Uhlén, “The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures,” Electrophoresis 26(3), 501–510 (2005).
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C. Cecconi, E. A. Shank, C. Bustamante, and S. Marqusee, “Direct Observation of the Three-State Folding of a Single Protein Molecule,” Science 309(5743), 2057–2060 (2005).
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Masaki, T.

H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
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H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
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J. Nilsson, M. Evander, B. Hammarström, and T. Laurell, “Review of cell and particle trapping in microfluidic systems,” Anal. Chim. Acta 649(2), 141–157 (2009).
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A. Holmberg, A. Blomstergren, O. Nord, M. Lukacs, J. Lundeberg, and M. Uhlén, “The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures,” Electrophoresis 26(3), 501–510 (2005).
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L. Novotny, R. X. Bian, and X. S. Xie, “Theory of nanometric optical tweezers,” Phys. Rev. Lett. 79(4), 645–648 (1997).
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N. C. Lindquist, J. Jose, S. Cherukulappurath, X. Chen, T. W. Johnson, and S. Oh, “Tip-based plasmonics: squeezing light with metallic nanoprobes,” Laser & Photon. Rev. 11, 1863–8899 (2013).

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K. Okamoto and S. Kawata, “Radiation force exerted on subwavelength particles near a nanoaperture,” Phys. Rev. Lett. 83(22), 4534–4537 (1999).
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Y. Pang and R. Gordon, “Optical Trapping of a Single Protein,” Nano Lett. 12(1), 402–406 (2012).
[Crossref] [PubMed]

Y. Pang and R. Gordon, “Optical Trapping of 12 nm Dielectric Spheres Using Double-Nanoholes in a Gold Film,” Nano Lett. 11(9), 3763–3767 (2011).
[Crossref] [PubMed]

M. Juan, R. Gordon, Y. Pang, F. Eftekhari, and R. Quidant, “Self-induced back-action optical trapping of dielectric nanoparticles,” Nat. Phys. 5(12), 915–919 (2009).
[Crossref]

Park, H.

Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire Nanosensors for Highly Sensitive and Selective Detection of Biological and Chemical Species,” Science 293(5533), 1289–1292 (2001).
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I. Ament, J. Prasad, A. Henkel, S. Schmachtel, and C. Sönnichsen, “Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles,” Nano Lett. 12(2), 1092–1095 (2012).
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M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
[Crossref] [PubMed]

M. L. Juan, M. Righini, and R. Quidant, “Plasmon nano-optical tweezers,” Nat. Photonics 5(6), 349–356 (2011).
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M. Juan, R. Gordon, Y. Pang, F. Eftekhari, and R. Quidant, “Self-induced back-action optical trapping of dielectric nanoparticles,” Nat. Phys. 5(12), 915–919 (2009).
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M. Nieto-Vesperinas, P. C. Chaumet, and A. Rahmani, “Near-field photonic forces,” Philos Trans A Math Phys Eng Sci 362(1817), 719–737 (2004).
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M. Geiselmann, M. L. Juan, J. Renger, J. M. Say, L. J. Brown, F. J. de Abajo, F. Koppens, and R. Quidant, “Three-dimensional optical manipulation of a single electron spin,” Nat. Nanotechnol. 8(3), 175–179 (2013).
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A. Zehtabi-Oskuie, H. Jiang, B. R. Cyr, D. W. Rennehan, A. A. Al-Balushi, and R. Gordon, “Double nanohole optical trapping: dynamics and protein-antibody co-trapping,” Lab Chip 13(13), 2563–2568 (2013).
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J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
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M. L. Juan, M. Righini, and R. Quidant, “Plasmon nano-optical tweezers,” Nat. Photonics 5(6), 349–356 (2011).
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I. Ament, J. Prasad, A. Henkel, S. Schmachtel, and C. Sönnichsen, “Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles,” Nano Lett. 12(2), 1092–1095 (2012).
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K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Trapping and rotating nanoparticles using a plasmonic nano-tweezer with an integrated heat sink,” Nat Commun 2, 469 (2011).
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K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Scannable Plasmonic Trapping Using a Gold Stripe,” Nano Lett. 10(9), 3506–3511 (2010).
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Y. F. Chen, X. Serey, R. Sarkar, P. Chen, and D. Erickson, “Controlled Photonic Manipulation of Proteins and Other Nanomaterials,” Nano Lett. 12(3), 1633–1637 (2012).
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E. A. Abbondanzieri, W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. M. Block, “Direct observation of base-pair stepping by RNA polymerase,” Nature 438(7067), 460–465 (2005).
[Crossref] [PubMed]

M. J. Lang, C. L. Asbury, J. W. Shaevitz, and S. M. Block, “An Automated Two-Dimensional Optical Force Clamp for Single Molecule Studies,” Biophys. J. 83(1), 491–501 (2002).
[Crossref] [PubMed]

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C. Cecconi, E. A. Shank, C. Bustamante, and S. Marqusee, “Direct Observation of the Three-State Folding of a Single Protein Molecule,” Science 309(5743), 2057–2060 (2005).
[Crossref] [PubMed]

Shevchenko, Y.

Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
[Crossref] [PubMed]

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J. T. Finer, R. M. Simmons, and J. A. Spudich, “Single myosin molecule mechanics: piconewton forces and nanometre steps,” Nature 368(6467), 113–119 (1994).
[Crossref] [PubMed]

Sönnichsen, C.

I. Ament, J. Prasad, A. Henkel, S. Schmachtel, and C. Sönnichsen, “Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles,” Nano Lett. 12(2), 1092–1095 (2012).
[Crossref] [PubMed]

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J. T. Finer, R. M. Simmons, and J. A. Spudich, “Single myosin molecule mechanics: piconewton forces and nanometre steps,” Nature 368(6467), 113–119 (1994).
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K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Trapping and rotating nanoparticles using a plasmonic nano-tweezer with an integrated heat sink,” Nat Commun 2, 469 (2011).
[Crossref] [PubMed]

K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Scannable Plasmonic Trapping Using a Gold Stripe,” Nano Lett. 10(9), 3506–3511 (2010).
[Crossref] [PubMed]

Strano, M. S.

J. H. Ahn, J. H. Kim, N. F. Reuel, P. W. Barone, A. A. Boghossian, J. Zhang, H. Yoon, A. C. Chang, A. J. Hilmer, and M. S. Strano, “Label-Free, Single Protein Detection on a Near-Infrared Fluorescent Single-Walled Carbon Nanotube/Protein Microarray Fabricated by Cell-Free Synthesis,” Nano Lett. 11(7), 2743–2752 (2011).
[Crossref] [PubMed]

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H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
[Crossref]

Tanaka, N.

H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
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Uhlén, M.

A. Holmberg, A. Blomstergren, O. Nord, M. Lukacs, J. Lundeberg, and M. Uhlén, “The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures,” Electrophoresis 26(3), 501–510 (2005).
[Crossref] [PubMed]

Walsh, R.

Y. Shevchenko, T. J. Francis, D. A. D. Blair, R. Walsh, M. C. DeRosa, and J. Albert, “In Situ Biosensing with a Surface Plasmon Resonance Fiber Grating Aptasensor,” Anal. Chem. 83(18), 7027–7034 (2011).
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K. Wang and K. B. Crozier, “Plasmonic Trapping with a Gold Nanopillar,” ChemPhysChem 13(11), 2639–2648 (2012).
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K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Trapping and rotating nanoparticles using a plasmonic nano-tweezer with an integrated heat sink,” Nat Commun 2, 469 (2011).
[Crossref] [PubMed]

K. Wang, E. Schonbrun, P. Steinvurzel, and K. B. Crozier, “Scannable Plasmonic Trapping Using a Gold Stripe,” Nano Lett. 10(9), 3506–3511 (2010).
[Crossref] [PubMed]

Wang, M. D.

M. D. Wang, H. Yin, R. Landick, J. Gelles, and S. M. Block, “Stretching DNA with Optical Tweezers,” Biophys. J. 72(3), 1335–1346 (1997).
[Crossref] [PubMed]

Wei, Q.

Y. Cui, Q. Wei, H. Park, and C. M. Lieber, “Nanowire Nanosensors for Highly Sensitive and Selective Detection of Biological and Chemical Species,” Science 293(5533), 1289–1292 (2001).
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A. Hoffmann, K. Neupane, and M. T. Woodside, “Single-molecule assays for investigating protein misfolding and aggregation,” Phys. Chem. Chem. Phys. 15(21), 7934–7948 (2013).
[Crossref] [PubMed]

W. J. Greenleaf, M. T. Woodside, E. A. Abbondanzieri, and S. M. Block, “Passive All-Optical Force Clamp for High-Resolution Laser Trapping,” Phys. Rev. Lett. 95(20), 208102 (2005).
[Crossref] [PubMed]

Xie, X. S.

L. Novotny, R. X. Bian, and X. S. Xie, “Theory of nanometric optical tweezers,” Phys. Rev. Lett. 79(4), 645–648 (1997).
[Crossref]

Yasokawa, T.

H. Kobayashi, I. Ishimaru, R. Hyodo, T. Yasokawa, K. Ishizaki, S. Kuriyama, T. Masaki, S. Nakai, K. Takegawa, and N. Tanaka, “A precise method for rotating single cells,” Appl. Phys. Lett. 88(13), 131103 (2006).
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Figures (5)

Fig. 1
Fig. 1 A schematic of the DNH optical trap with dual microfluidic input. Abbreviations used: ODF = optical density filter; HWP = half-wave plate; BE = beam expander; MR = mirror; MO = microscope objective; OI MO = oil immersion objective; APD = avalanche photodetector.
Fig. 2
Fig. 2 A schematic showing the protein binding experiments .(a) 20 nm biotin-coated PS particle approaches the DNH. (b) Introduction of streptavidin to the trapping site once a successful trapping event of 20 nm biotin-coated PS particle is achieved. (c) Streptavidin is bound to biotin between the two sharp cusps of the DNH. (d) A scanning electron microscope image of the DNH used in the protein binding and control experiments.
Fig. 3
Fig. 3 Time trace of optical transmission through the DNH where (a) shows flowing 20 nm biotin-coated PS particles through the microfluidic channel, (b) trapping of 20 nm biotin-coated PS particle between the two sharp tips formed by two overlapping DNHs and subsequently flowing streptavidin, and (c) binding between 20 nm biotin-coated PS particle and streptavidin.
Fig. 4
Fig. 4 Time trace of optical transmission through the DNH for the saturated streptavidin control experiment where (a) shows flowing 20 nm biotin-coated PS particles through the microfluidic channel, (b) trapping of 20 nm biotin-coated PS particle between the cusps of the DNH and subsequently flowing saturated streptavidin, and (c) saturated streptavidin does not bind to the trapped 20 nm biotin-coated PS particle.
Fig. 5
Fig. 5 Time trace of optical transmission through the DNH for the non-functionalized PS particle control experiment where (a) shows flowing 20 nm PS particles through the microfluidic channel, (b) trapping of 20 nm PS particle between the cusps of the DNH and subsequently flowing streptavidin, and (c) streptavidin does not bind to the trapped 20 nm PS particle.

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