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Protein Assembly Through Site-specific Interactions with Gold Nanoparticles

Published online by Cambridge University Press:  01 February 2011

Minghui Hu ,
Luping Qian ,
Raymond P Briñas ,
Elena S Lymar  and
James F Hainfeld
Minghui Hu
Affiliation:
[email protected], Brookhaven National Laboratory, Biology Department, Brookhaven National Laboratory, Upton, NY, 11973, United States, 631 344 3747, 631 344 3407
Luping Qian
Affiliation:
[email protected], Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
Raymond P Briñas
Affiliation:
[email protected], Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
Elena S Lymar
Affiliation:
[email protected], Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
James F Hainfeld
Affiliation:
[email protected], Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
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Abstract

A universal method is described to design and construct protein-nanoparticle assemblies controlled by nanoparticle functionality, and placement of genetic tag into proteins. Well-defined binding complexes of nanoparticles and two proteins, the adenovirus serotype 12 knob and the mycobacterium tuberculosis 20S proteasome, were formed through site-specific binding between 6x-histidine tags in proteins and nickel-nitrilotriacetic acid functional groups on gold nanoparticles.

Keywords

nanostructurebiological synthesis (assembly)transmission electron microscopy (TEM)
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 951: Symposium E – Nanofunctional Materials, Nanostructures and Novel Devices for Biological and Chemical Detection , 2006 , 0951-E10-10
Copyright
Copyright © Materials Research Society 2007

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References

REFERENCES

1. Niemeyer, C. M., Angew. Chem. Int. Ed. 40, 4128 (2001).Google Scholar
2. Whitesides, G. M., Boncheva, M., Proc. Natl. Acad. Sci. U. S. A. 99, 4769 (2002).Google Scholar
3. Vertegel, A. A., Siegel, R. W., Dordick, J. S., Langmuir 20, 6800 (2004).Google Scholar
4. Ackerson, C. J., Sykes, M. T., Kornberg, R. D., Proc. Natl. Acad. Sci. U. S. A. 102, 13383 (2005).Google Scholar
5. Srivastava, S., Verma, A., Frankamp, B. L., Rotello, V. M., Adv. Mater. 17, 617 (2005).Google Scholar
6. Tseng, R. J., Tsai, C., Ma, L., Ouyang, J., Ozkan, C. S., Yang, Y., Nat. Nanotechnol. 1, 72 (2006).Google Scholar
7. You, C., Agasti, S. S., De, M., Knapp, M. J., Rotello, V. M., J. Am. Chem. Soc. 128, 14612 (2006).Google Scholar
8. Raymond, B. P., Hu, M., Qian, L., Lymar, E. S., Hainfeld, J. F., In preparation (2006).Google Scholar
9. Roure, O. Du, Debiemme-Chouvy, C., Malthete, J., Silberzan, P., Langmuir 19, 4138 (2003).Google Scholar
10. Bewley, M. C., Springer, K., Zhang, Y., Freimuth, P., Flanagan, J. M., Science 286, 1579 (1999).Google Scholar
11. Hu, G. Q., Lin, G., Wang, M., Dick, L., Xu, R., Nathan, C., Li, H. L., Mol. Microbiol. 59, 1417 (2006).Google Scholar
12. Hu, M., Qian, L., Raymond, B. P., Lymar, E. S., Hainfeld, J. F., submitted to Angew. Chem. Int. Ed. (2007).Google Scholar