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Borrowing Ideas from Nature: Peptide Specific Binding to Gallium Arsenide

Published online by Cambridge University Press:  10 February 2011

Sandra R. Whaley
Affiliation:
Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin TX 78712, USA
Angela M. Belcher
Affiliation:
Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin TX 78712, USA The Texas Materials Institute, The University of Texas at Austin, Austin TX 78712, USA belcher @mail.utexas.edu
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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.

Type
Research Article
Copyright
Copyright © Materials Research Society 2000

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