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Optimal dye-quencher pairs for the design of an “activatable” nanoprobe for optical imaging

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Abstract

Optical imaging offers high sensitivity and portability at low cost. The design of an optimal “activatable” imaging agent could greatly decrease the background noise and increase specificity of the signal. Five different molecules have been used to quench basal fluorescence of an enzyme substrate labeled with Cy5, Cy5.5 or IR800 at a distance of 8 amino acids (32 Å): a 6 nm gold nanoparticle (NP), a 20 nm and a 30 nm iron oxide (FeO) NP, the black hole quencher BHQ-3 and the IRdye quencher QC-1. The quenching efficiencies were 99% for QC1-IR800, 98% for QC1-Cy5.5, 96% for 30 nm FeO NP-Cy5.5, 89% for BHQ3-Cy5, 84% for BHQ3-Cy5.5, 77-90% for 6 nm gold NP-Cy5.5, depending on the number of dyes around the NP, 79% for 20 nm FeO NP-Cy5.5 and 77% for Cy5.5-Cy5. Signal activation upon cleavage by the matrix metalloproteinase MMP9 was proportional to the quenching efficiencies, ranging from 3-fold with Cy5.5-Cy5 to 67-fold with QC1-IR800. This independent work reports on the properties of the dyes and quenchers explaining the superior performance of QC-1 and 30 nm FeO NPs.

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Notes and references

  1. S. Netzel-Arnett, S. K. Mallya, H. Nagase, H. Birkedal-Hansen, H. E. Van Wart, Anal. Biochem., 1991, 195, 86–92.

    Article  CAS  Google Scholar 

  2. W. R. Algar, A. P. Malanoski, K. Susumu, M. H. Stewart, N. Hildebrandt and I. L. Medintz, Anal. Chem., 2012, 84, 10136–10146.

    Article  CAS  Google Scholar 

  3. K. Boeneman, B. C. Mei, A. M. Dennis, G. Bao, J. R. Deschamps, H. Mattoussi and I. L. Medintz, J. Am. Chem. Soc., 2009, 131, 3828–3829.

    Article  CAS  Google Scholar 

  4. I. L. Medintz, A. R. Clapp, F. M. Brunel, T. Tiefenbrunn, H. T. Uyeda, E. L. Chang, J. R. Deschamps, P. E. Dawson and H. Mattoussi, Nat. Mater., 2006, 5, 581–589.

    Article  CAS  Google Scholar 

  5. I. L. Medintz, M. H. Stewart, S. A. Trammell, K. Susumu, J. B. Delehanty, B. C. Mei, J. S. Melinger, J. B. Blanco-Canosa, P. E. Dawson and H. Mattoussi, Nat. Mater., 2010, 9, 676–684.

    Article  CAS  Google Scholar 

  6. J. Han, A. Loudet, R. Barhoumi, R. C. Burghardt and K. Burgess, J. Am. Chem. Soc., 2009, 131, 1642–1643.

    Article  CAS  Google Scholar 

  7. M. K. Johansson, H. Fidder, D. Dick and R. M. Cook, J. Am. Chem. Soc., 2002, 124, 6950–6956.

    Article  CAS  Google Scholar 

  8. M. Ogawa, N. Kosaka, P. L. Choyke and H. Kobayashi, ACS Chem. Biol., 2009, 4, 535–546.

    Article  CAS  Google Scholar 

  9. S. Prahl, compiled from the data provided by W. B. Gratzer and N. Kollias, Available at http://omlc.ogi.edu/spectra/hemoglobin/summary.html.

  10. G. M. Hale and M. R. Querry, Appl. Opt., 1973, 12, 555–563.

    Article  CAS  Google Scholar 

  11. A. Mishra, R. K. Behera, P. K. Behera, B. K. Mishra and G. B. Behera, Chem. Rev., 2000, 100, 1973–2012.

    Article  CAS  Google Scholar 

  12. C. S. Yun, A. Javier, T. Jennings, M. Fisher, S. Hira, S. Peterson, B. Hopkins, N. O. Reich and G. F. Strouse, J. Am. Chem. Soc., 2005, 127, 3115–3119.

    Article  CAS  Google Scholar 

  13. X. Liu, M. Atwater, J. Wang and Q. Huo, Colloids Surf., B: Biointerfaces, 2007, 58, 3–7.

    Article  CAS  Google Scholar 

  14. Y. Q. He, S. P. Liu, L. Kong and Z. F. Liu, Spectrochim. Acta, Part A, 2005, 61, 2861–2866.

    Article  Google Scholar 

  15. P. Ray, G. Darbha, A. Ray, J. Walker and W. Hardy, Plasmonics, 2007, 2, 173–183.

    Article  CAS  Google Scholar 

  16. M. Ogawa, C. A. Regino, P. L. Choyke and H. Kobayashi, Mol. Cancer Ther., 2009, 8, 232–239.

    Article  CAS  Google Scholar 

  17. M. Ogawa, N. Kosaka, P. L. Choyke and H. Kobayashi, Cancer Res., 2009, 69, 1268–1272.

    Article  CAS  Google Scholar 

  18. F. A. Jaffer, D. E. Kim, L. Quinti, C. H. Tung, E. Aikawa, A. N. Pande, R. H. Kohler, G. P. Shi, P. Libby and R. Weissleder, Circulation, 2007, 115, 2292–2298.

    Article  CAS  Google Scholar 

  19. X. Peng, H. Chen, D. R. Draney, W. Volcheck, A. Schutz-Geschwender and D. M. Olive, Anal. Biochem., 2009, 388, 220–228.

    Article  CAS  Google Scholar 

  20. C. Bremer, S. Bredow, U. Mahmood, R. Weissleder and C. H. Tung, Radiology, 2001, 221, 523–529.

    Article  CAS  Google Scholar 

  21. I. Selo, L. Negroni, C. Creminon, J. Grassi and J. M. Wal, J. Immunol. Methods, 1996, 199, 127–138.

    Article  CAS  Google Scholar 

  22. S. J. Kridel, E. Chen, L. P. Kotra, E. W. Howard, S. Mobashery and J. W. Smith, J. Biol. Chem., 2001, 276, 20572–20578.

    Article  CAS  Google Scholar 

  23. A. Prudova, U. auf dem Keller, G. S. Butler and C. M. Overall, Mol. Cell Proteomics, 2010, 9, 894–911.

    Article  CAS  Google Scholar 

  24. M. K. Johansson, Methods Mol. Biol., 2006, 335, 17–29.

    CAS  PubMed  Google Scholar 

  25. R. Lebel, M. A. Bonin, R. Zriba, A. Radulska, W. Neugebauer and M. Lepage, Contrast. Media Mol. Imaging, 2012, 7, 328–337.

    Article  CAS  Google Scholar 

  26. K. E. Adams, S. Ke, S. Kwon, F. Liang, Z. Fan, Y. Lu, K. Hirschi, M. E. Mawad, M. A. Barry, E. M. Sevick-Muraca, J. Biomed. Opt., 2007, 12, 024017.

    Article  Google Scholar 

  27. K. E. Linder, E. Metcalfe, P. Nanjappan, T. Arunachalam, K. Ramos, T. M. Skedzielewski, E. R. Marinelli, M. F. Tweedle, A. D. Nunn and R. E. Swenson, Bioconjug. Chem., 2011, 22, 1287–1297.

    Article  CAS  Google Scholar 

  28. L. Niedzwiecki, J. Teahan, R. K. Harrison and R. L. Stein, Biochemistry, 1992, 31, 12618–12623.

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, 451 Smyth Road, Ottawa, Ontario, Canada

    Bryan Simard

  2. Department of Clinical Neurosciences and Radiology, University of Calgary, 3330 Hospital Dr NW, Calgary, Alberta, Canada

    Boguslaw Tomanek

  3. Department of Chemistry, University of Victoria, P.O. Box 3065, Victoria, British Columbia, Canada

    Frank C. J. M. van Veggel

  4. Institute for Biological Sciences, National Research Council of Canada, 1200 Montreal Road, Ottawa, Ontario, Canada

    Abedelnasser Abulrob

Authors
  1. Bryan Simard
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  2. Boguslaw Tomanek
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  3. Frank C. J. M. van Veggel
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  4. Abedelnasser Abulrob
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Correspondence to Abedelnasser Abulrob.

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Simard, B., Tomanek, B., van Veggel, F.C.J.M. et al. Optimal dye-quencher pairs for the design of an “activatable” nanoprobe for optical imaging. Photochem Photobiol Sci 12, 1824–1829 (2013). https://doi.org/10.1039/c3pp50118c

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  • DOI: https://doi.org/10.1039/c3pp50118c

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