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Integration of Biomolecules with Inorganic Ferroelectrics: A Novel Approach to Nanoscale Devices

Published online by Cambridge University Press:  01 February 2011

Brian Reiss
Affiliation:
firestone@anl.gov, Argonne National Laboratory, Materials Science Division, 9700 South Cass Avenue, Argonne, IL, 60349, United States, 630-252-8298
Orlando Auciello
Affiliation:
orlando@anl.gov, Argonne National Laboratory, Materials Science Division, 9700 South Cass Avenue, Argonne, IL, 60439, United States
Leonidas E. Ocola
Affiliation:
ocola@anl.gov, Argonne National Laboratory, Center for Nanoscale Materials, Argonne, IL, 60439, United States
Millicent Anne Firestone
Affiliation:
firestone@anl.gov, Argonne National Laboratory, Materials Science Division, 9700 South Cass Avenue, Argonne, IL, 60349, United States
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Abstract

In this work, we investigate the feasibility of using a surface-tethered heptapeptide sequence as the basis for a ferroelectric-actuated component in a nanofluidic device. The fluorescently-labeled peptide sequence, (CISLLHSTC) is shown by fluorescence microscopy to selectively coat the PZT patterned channel floors. The peptide binding strength to PZT is determined over a range of flow rates in the patterned channel by imaging the fluorescence intensity of the coated channel and monitoring the output spectroscopically. The peptide is found to be stripped from the PZT at flow rates exceeding 5mL/h. Initial results demonstrating the possibility of covalently integrating the short peptide sequence to larger biological components such as antibodies are also presented.

Type
Research Article
Copyright
Copyright © Materials Research Society 2007

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References

REFERENCES

1 Whitesides, G. M. and Wong, A. P., MRS Bulletin 31, 1927 (2006).Google Scholar
2 Patolsky, F., Zheng, G., and Lieber, C. M., Nanomedicine 1, 5165 (2006).Google Scholar
3 Martin, C. R. and Aksay, I. A., Journal of Physical Chemistry B 107, 42614268 (2003).Google Scholar
4 Scott, J. F. and Dearaujo, C. A. P., Science 246, 14001405 (1989).Google Scholar
5 Auciello, O., Scott, J. F., and Ramesh, R., Physics Today 51, 2227 (1998).Google Scholar
6 Reiss, B. D., Bai, G. R., Auciello, O., Ocola, L. E., and Firestone, M. A., Applied Physics Letters 88, 083903 (2006).Google Scholar
7 Reiss, B. D., Ocola, L. E., Auciello, O., and Firestone, M. A., Mater. Res. Soc. Symp. Proc. 944, 094-AA02-08 (2006).Google Scholar
8 Ocola, L. E., Pan, W. C., Kuo, M., Tirumala, V. R., Reiss, B. D., Firestone, M. A., and Auciello, O., NSTI-Nanotech 2005 3, 439442 (2005).Google Scholar
9 Yi, G., Wu, Z., and M., S., J. Appl. Phys. 64, 27172724 (1988).Google Scholar
10 Xia, Y. and Whitesides, G. M., Angew. Chem. Int. Ed. Engl. 37, 550575 (1998).Google Scholar
11 Atherton, E. and Sheppard, R. C., Solid Phase Peptide Synthesis: A Practical Approach (IRL Press, Oxford, 1989).Google Scholar
12 Smith, G. P. and Petrenko, V. A., Chem. Rev. 97, 391 (1997).Google Scholar