Nanotube-assisted protein deactivation

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Abstract

Conjugating proteins onto carbon nanotubes has numerous applications in biosensing1,2, imaging and cellular delivery3,4,5. However, remotely controlling the activity of proteins in these conjugates has never been demonstrated. Here we show that upon near-infrared irradiation, carbon nanotubes mediate the selective deactivation of proteins in situ by photochemical effects. We designed nanotube–peptide conjugates to selectively destroy the anthrax toxin, and also optically transparent coatings that can self-clean following either visible or near-infrared irradiation. Nanotube-assisted protein deactivation may be broadly applicable to the selective destruction of pathogens and cells, and will have applications ranging from antifouling coatings to functional proteomics.

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Figure 1: Behaviour of nanotube and nanotube–protein conjugates after NIR irradiation.
Figure 2: Deactivation behaviour of nanotube–protein conjugates.
Figure 3: Functionalizing carbon nanotubes with peptides that recognize anthrax toxin.
Figure 4: Applications of nanotube-assisted protein deactivation.

References

  1. 1

    Chen, R. J. et al. Noncovalent functionalization of carbon nanotubes for highly specific electronic biosensors. Proc. Natl Acad. Sci. USA 100, 4984–4989 (2003).

  2. 2

    Barone, P. W., Baik, S., Heller, D. A. & Strano, M. S. Near-infrared optical sensors based on single-walled carbon nanotubes. Nature Mater. 4, 86–92 (2005).

  3. 3

    Bianco, A., Kostarelos, K., Partidos, C. D. & Prato, M. Biomedical applications of functionalised carbon nanotubes. Chem. Commun. 571–577 (2005).

  4. 4

    Kam, N. W. S., O'Connell, M., Wisdom, J. A. & Dai, H. Carbon nanotubes as multifunctional biological transporters and near-infrared agents for selective cancer cell destruction. Proc. Natl Acad. Sci. USA 102, 11600–11605 (2005).

  5. 5

    Liu, Z. et al. In vivo biodistribution and highly efficient tumour targeting of carbon nanotubes in mice. Nature Nanotech. 2, 47–52 (2006).

  6. 6

    Hirsch, L. R. et al. Nanoshell-mediated near-infrared thermal therapy of tumors under magnetic resonance guidance. Proc. Natl Acad. Sci. USA 11, 13549–13554 (2003).

  7. 7

    Zheng, M. & Rostovtsev, V. V. Photoinduced charge transfer mediated by DNA-wrapped carbon nanotubes. J. Am. Chem. Soc. 128, 7702–7703 (2006).

  8. 8

    Bosi, S., Da Ros, T., Spalluto, G. & Prato, M. Fullerene derivatives: an attractive tool for biological applications. Eur. J. Med. Chem. 38, 913–923 (2003).

  9. 9

    Yamakoshi, Y. et al. Active oxygen species generated from photoexcited fullerene (C60) as potential medicines: O2−. versus 1O2 . J. Am. Chem. Soc. 125, 12803–12809 (2003).

  10. 10

    Bakalova, R. et al. Quantum dot anti-CD conjugates: Are they potential photosensitizers or potentiators of classical photosensitizing agents in photodynamic therapy of cancer? Nano Lett. 4, 1567–1573 (2004).

  11. 11

    Bakalova, R., Ohba, H., Zhelev, Z., Ishikawa, M. & Baba, Y. Quantum dots as photosensitizers? Nature Biotechnol. 22, 1360–1361 (2004).

  12. 12

    Keblinski, P., Cahill, D. G., Bodapati, A., Sullivan, C. R. & Taton, T. A. Limits of localized heating by electromagnetically excited nanoparticles. J. Appl. Phys. 100, 54305 (2006).

  13. 13

    Bulina, M. E. et al. A genetically encoded photosensitizer. Nature Biotechnol. 24, 95–99 (2006).

  14. 14

    Davies, K. J. A. Protein damage and degradation by oxygen radicals. J. Biol. Chem. 262, 9895–9901 (1987).

  15. 15

    Izumi, I., Fan, F.-R. F. & Bard, A. J. Heterogeneous photocatalytic decomposition of benzoic acid and adipic acid on platinized TiO2 powder. The photo-Kolbe decarboxylative route to the breakdown of the benzene ring and to the production of butane. J. Phys. Chem. 85, 218–223 (1981).

  16. 16

    Dukovic, G. et al. Reversible surface oxidation and efficient luminescence quenching in semiconductor single-wall carbon nanotubes. J. Am. Chem. Soc. 126, 15269–15276 (2004).

  17. 17

    Strano, M. S. et al. Reversible, band-gap-selective protonation of single-walled carbon nanotubes in solution. J. Phys. Chem. B 107, 6979–6985 (2003).

  18. 18

    Koppenol, W. H. & Butler, J. Energetics of interconversion of oxyradicals. Adv. Free Radic. Biol. Medic. 1, 81–131 (1985).

  19. 19

    Okazaki, K., Nakato, Y. & Murakoshi, K. Absolute potential of the Fermi level of isolated single-walled carbon nanotubes. Phys. Rev. B 68, 035434 (2003).

  20. 20

    Zheng, M. & Diner, B. A. Solution redox chemistry of carbon nanotubes. J. Am. Chem. Soc. 126, 15490–15496 (2004).

  21. 21

    Bottini, M. et al. Full-length single-walled carbon nanotubes decorated with streptavidin-conjugated quantum dots as multivalent intracellular fluorescent nanoprobes. Biomacromolecules 7, 2259–2263 (2006).

  22. 22

    Gu, L. et al. Single-walled carbon nanotubes displaying multivalent ligands for capturing pathogens. Chem. Commun. 874–876 (2005).

  23. 23

    Rai, P. et al. Statistical pattern matching facilitates the design of polyvalent inhibitors of anthrax and cholera toxins. Nature Biotechnol. 24, 582–586 (2006).

  24. 24

    Wu, Z. et al. Transparent, conductive carbon nanotube films. Science 305, 1273–1276 (2004).

  25. 25

    Parkin, I. P. & Palgrave, R. G. Self-cleaning coatings. J. Mater. Chem. 15, 1689–1695 (2005).

  26. 26

    Karajanagi, S. S., Vertegel, A. A., Kane, R. S. & Dordick, J. S. Structure and function of enzymes adsorbed onto single-walled carbon nanotubes. Langmuir 20, 11594–11599 (2004).

  27. 27

    Asuri, P. et al. Water-soluble carbon nanotube–enzyme conjugates as functional biocatalytic formulations. Biotech. Bioeng. 95, 804–811 (2006).

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Acknowledgements

We acknowledge support from the National Institutes of Health (U01 AI056546) and the National Science Foundation (DMR 0642573, CBET 0348613). We also thank R. Planty for assistance with the X-ray photoelectron spectroscopy measurements.

Author information

A.J. and S.P. designed and performed the experiments, analysed the data, and co-wrote the manuscript. S.S.B. and H.Y. carried out TEM imaging. T.B.-T. designed the experiments. R.S.K. conceived and designed the experiments, analysed the data and wrote the manuscript. All authors discussed the results and commented on the manuscript.

Correspondence to Ravi S. Kane.

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Supplementary figures S1–S7 (PDF 419 kb)

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Joshi, A., Punyani, S., Bale, S. et al. Nanotube-assisted protein deactivation. Nature Nanotech 3, 41–45 (2008) doi:10.1038/nnano.2007.386

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