Hostname: page-component-78c5997874-ndw9j Total loading time: 0 Render date: 2024-11-02T23:14:38.760Z Has data issue: false hasContentIssue false
  • English
  • Français

Nanowiring Enzymes to Carbon Nanotube Probes

Published online by Cambridge University Press:  17 March 2011

C.P. Collier ,
M.J. Esplandiu ,
V.G. Bittner  and
I.R. Shapiro
C.P. Collier
Affiliation:
California Institute of Technology Division of Chemistry and Chemical Engineering
M.J. Esplandiu
Affiliation:
California Institute of Technology Division of Chemistry and Chemical Engineering
V.G. Bittner
Affiliation:
California Institute of Technology Division of Chemistry and Chemical Engineering
I.R. Shapiro
Affiliation:
California Institute of Technology Division of Chemistry and Chemical Engineering
Get access

Abstract

The observation of spectroscopic signals in response to mechanically induced changes in biological macromolecules can be enabled at an unprecedented level of resolution by coupling single-molecule manipulation/sensing using carbon nanotubes with single-molecule fluorescence imaging. Proteins, DNA and other biomolecules can be attached to nanotubes to give highly specific single-molecule probes for the investigation of intermolecular dynamics, the assembly of hybrid biological and nanoscale materials and the development of molecular electronics. Recent advances in nanotube fabrication and Atomic Force Microscope (AFM) imaging with nanotube tips have demonstrated the potential of these tools to achieve high-resolution images of single molecules. In addition, proof-of-principle demonstrations of nanotube functionalization and attachment of single molecules to these probes have been successfully made.

Improved techniques for the growth and attachment of single wall carbon nanotubes as robust and well-characterized tools for AFM imaging are being developed. This work serves as a foundation toward development of single-molecule sensors and manipulators on nanotube AFM tips for a hybrid atomic force microscope that also has single-molecule fluorescence imaging capability. An individual single wall carbon nanotube (SWNT) attached to an AFM tip can function as a structural scaffold for nanoscale device fabrication on a scanning probe. Such a probe can have a novel role, to trigger specific biochemical reactions or conformational changes in a biological system with nanometer precision. The consequences of these perturbations can be read out in real time by single-molecule fluorescence and/or AFM sensing. For example, electrical wiring of single redox enzymes to carbon nanotube scanning probes will allow for observation and electrochemical control of single enzymatic reactions, by monitoring fluorescence from a redox-active cofactor or the formation of fluorescent products. Enzymes “nanowired” to carbon nanotube tips may enable extremely sensitive probing of biological stimulus-response with high spatial resolution, including product-induced signal transduction.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 823: Symposium W – Biological and Bioinspired Materials and Devices , 2004 , W8.7
Copyright
Copyright © Materials Research Society 2004

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Ishijima, A.; Yanagida, T.: Trends Biochem. Sci. 26, 438 (2001).CrossRefGoogle Scholar
2. Bustamante, C.; Macosko, J.C.; Wuite, G.J.L.: Nat. Rev. Mol. Cell Biol. 1, 130 (2000).CrossRefGoogle Scholar
3. Hafner, J.H.; Cheung, C.-L.; Wooley, A.T.; Leiber, C.M.: Prog. Biophys. Mol. Biol. 77, 73 (2001).CrossRefGoogle Scholar
4. Wong, S.S.; Joselevich, E.; Wooley, A.T.; Cheung, C.-L.; Lieber, C.M.: Nature 394, 52 (1998).CrossRefGoogle Scholar
5. Chen, R., Bangsaruntip, S., Drouvalakis, K., Kam, N.W.S., Shim, M., Li, Y., Kim, W., Utz, P., and Dai, H., Proc. Natl. Acad. Sci. USA 100, 4984 (2003).CrossRefGoogle Scholar
6. Schütz, G., Sonnleitner, M., Hinterdorfer, P., and Schindler, H., Mol. Membrane Bio. 17, 17 (2000).CrossRefGoogle Scholar
7. Fiorini, M., McKendry, R., Cooper, M., Rayment, T., and Abell, C., Biophys. J. 80, 2471 (2001).CrossRefGoogle Scholar
8. Sun, B. and Chiu, D.T., J. Am. Chem. Soc. 125, 3702 (2003).CrossRefGoogle Scholar
9. Groves, J.T. and Boxer, S.G., Acc. Chem. Res. 35, 149 (2002).CrossRefGoogle Scholar
10. Pantoja, R., Sigg, D., Blunck, R., Bezanilla, F., and Heath, J.R., Biophys. J. 81, 2389 (2001).CrossRefGoogle Scholar
11. Li, Y., Kim, W., Zhang, Y., Rolandi, M., Wang, D., and Dai, H., J. Phys. Chem. B 105, 11424 (2001).CrossRefGoogle Scholar
12. Hafner, J.H., Cheung, C.-L., Oosterkamp, T.H., and Lieber, C.M., J. Phys. Chem. B 105, 743 (2001).CrossRefGoogle Scholar
13. Wade, L., Shapiro, I., Ma, Z., Quake, S.R., and Collier, C.P., Nano Lett. 4, 725 (2004).CrossRefGoogle Scholar
14. Wade, L., Shapiro, I., Ma, Z., Quake, S. and Collier, C. P., Nanotech 2003 3, 317 (2003).Google Scholar
15. Losito, I., Palmisano, F., and Zambonin, P.G., Anal. Chem. 75, 4988 (2003).CrossRefGoogle Scholar
16. Wilson, N.R., Cobden, D.H., and MacPherson, J.V., J. Phys. Chem. B 106, 13102 (2002).CrossRefGoogle Scholar
17. Heller, A., J. Phys. Chem. 96, 3579 (1992).CrossRefGoogle Scholar
18. Xiao, Y., Patolsky, F., Katz, E., Hainfeld, J.F., and Willner, I., Science 299, 1877 (2003).CrossRefGoogle Scholar