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 OSA

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

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]

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.

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[Crossref] [PubMed]

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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).
[Crossref] [PubMed]

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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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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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