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Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly

Nature volume 405, pages 665–668 (2000)Cite this article

Abstract

In biological systems, organic molecules exert a remarkable level of control over the nucleation and mineral phase of inorganic materials such as calcium carbonate and silica, and over the assembly of crystallites and other nanoscale building blocks into complex structures required for biological function1,2,3,4. This ability to direct the assembly of nanoscale components into controlled and sophisticated structures has motivated intense efforts to develop assembly methods that mimic or exploit the recognition capabilities and interactions found in biological systems5,6,7,8,9,10. Of particular value would be methods that could be applied to materials with interesting electronic or optical properties, but natural evolution has not selected for interactions between biomolecules and such materials. However, peptides with limited selectivity for binding to metal surfaces and metal oxide surfaces have been successfully selected10,11. Here we extend this approach and show that combinatorial phage-display libraries can be used to evolve peptides that bind to a range of semiconductor surfaces with high specificity, depending on the crystallographic orientation and composition of the structurally similar materials we have used. As electronic devices contain structurally related materials in close proximity, such peptides may find use for the controlled placement and assembly of a variety of practically important materials, thus broadening the scope for ‘bottom-up’ fabrication approaches.

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Figure 1: Selected amino-acid sequences of randomized peptide inserts.
Figure 2: Detection of gold-labelled phage on GaAs using X-ray photoelectron spectroscopy.
Figure 3: AFM and TEM analysis of peptide–semiconductor recognition.
Figure 4: Phage recognition of semiconductor heterostructures.

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Acknowledgements

We thank D. Margolese, D. Morse and G. Stucky for discussions, and H. Reese, J. English and R. Naone for providing semiconductor substrates. We acknowledge the use of the core microscopy facilities in the Texas Materials Institute (SEM). We also thank the Institute of Molecular and Cellular Biology (TEM) at the University of Texas at Austin. We acknowledge the assistance of the NSF-sponsored National Nanofabrication Users Network in providing some of the structures for this project. This work was supported by ARO/DARPA (S.R.W and A.M.B), a DuPont Young Investigator Award (A.M.B.), the NSF (P.F.B. and E.L.H.) and the Robert A. Welch Foundation (P.F.B. and A.M.B.). This work was also funded by faculty start-up funds provided by the University of Texas at Austin (A.M.B.).

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry,

    Sandra R. Whaley, D. S. English, Paul F. Barbara & Angela M. Belcher

  2. The Texas Materials Institute, The University of Texas at Austin, Austin, 78712, Texas, USA

    Paul F. Barbara & Angela M. Belcher

  3. Center for Quantized Electronic Structures, University of California, Santa Barbara, 93106, California, USA

    Evelyn L. Hu

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  1. Sandra R. Whaley
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Correspondence to Angela M. Belcher.

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Whaley, S., English, D., Hu, E. et al. Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly. Nature 405, 665–668 (2000). https://doi.org/10.1038/35015043

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