Skip to main content Accessibility help
×
Home

Borrowing Ideas from Nature: Peptide Specific Binding to Gallium Arsenide

  • Sandra R. Whaley (a1) and Angela M. Belcher (a1) (a2) (a3)

Abstract

Biological systems have a unique ability to control crystal structure, phase, orientation and nanostructural regularity of inorganic materials. An example is seen with the control of crystallographic phase and orientation of calcium carbonate with the polyanionic proteins isolated from shells of the marine gastropod abalone. We are currently investigating the principles of natural biological molecular recognition in materials and developing new methods to pattern useful non-biological electronic and magnetic materials on new length scales. A peptide combinatorial approach has been employed to identify proteins that select for and specifically bind to inorganic structures such as semiconductor wafers, nanoparticles and quantum confined structures. This approach utilizes the inherent self-organizing, highly selective properties of biologically derived molecules. We are currently investigating peptide recognition and interaction with III-V and II-VI semiconductor materials, magnetic materials, calcium carbonates and phosphates. We have selected peptides that can specifically bind and discriminate between zinc-blende III-V semiconductor surfaces. These peptides show crystal face specificity and are being used to organize nanoparticle heterostructures. Long term potential application of these materials would include opto-electronic devices such as light emitting displays, optical detectors, lasers, and nanometer scale computer components.

Copyright

References

Hide All
1. Colvin, V.L, Goldstein, A.N., Alivisators, A.P, Journ. Ameri. Chem. Soc. 144 (13), 5221 (1992).
2. Brust, M., Bethell, D., Schiffrin, D.J., Kiely, C.J., Adv. Mater. 7 (9), 795 (1995).
3. Li, M., Wong, K. K. W., Mann, S., Chem. Mater. 11 23, (1999).
4. Alivisatos, A. P., et al., Nature 382, 609 (1996).
5. Mirkin, R. L., el al., Nature 382, 607 (1996).
6. Belcher, A.M. et al., Nature 381, 56 (1996).
7. Falina, G., et al., Science 271, 67 (1996).
8. Cha, J.N, el al., Proc. Natl.Acad Sci, V96 N2:361365 (1999). 198
9. Parmley, S. F., and Smith, G. P., Gene 73, 305 (1988).
10. New England Biolabs, Beverly, MA, USA.
11. Brown, S., Proc. Natl.Acad Sci 89, 8651 (1992).
12. Brown, S., Nature Biotechnology 15, 269 (1997).
13. GaAs (100) from Freiberger, undoped, GaAs (111)A and (111)B Wafer Technology Limited, undoped, and Si from MEMC, InP (100).
14. Swaminathan, V., and Macrander, A.T., in Materials Aspects of GaAs and InP Based Structures, (Prentice Hall, 1991).
15. The authors would like to thank Dr. David Margolese and Dr. Evelyn Hu for helpful discussions and Helen Reese, John English, Ryan Naone for providing semiconductor substrates. This work was supported by an ARO/DARPA grant DAAD 199910155 (S.R.W and A.M.B), a Dreyfus Fellowship (S.R.W.) and DuPont Young Investigator Award (A.M.B.). This work was also funded by faculty start-up funds provided by the University of Texas at Austin (A.M.B.).

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed