Ferroelectric-Specific Peptides as Building Blocks for Bio-Inorganic Devices
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0944-AA02-08
Ferroelectric-Specific Peptides as Building Blocks for Bio-Inorganic Devices Brian Dennis Reiss1,2, Leonidas Ocola1, Orlando Auciello1,2, and Millicent A. Firestone1,2 1 Center for Nanoscale Materials, Argonne National Laboratory, 9700 S. Cass Ave., Argonne, IL, 60439 2 Materials Science Division, Argonne National Laboratory, 9700 S. Cass Ave., Argonne, IL, 60439
ABSTRACT The integration of biomolecules with inorganic materials to create functional composites represents a critical step in the development of next-generation biosensors, micro/nanofluidic devices, and biochips that require a combination of abiotic (inorganics) and biotic (proteins, DNA, antibodies) components. Toward this end, we have previously applied combinatorial phage display techniques to identify a constrained heptapeptide sequence (CISLLHSTC) that selectively binds to a perovskite ferroelectric (MOCVD-deposited lead zirconium titanate, PZT). In this work, we examine the binding of this heptapeptide sequence, prepared by solid phase peptide synthesis to sol-gel PZT. In particular, the surface roughness has been examined and the long-term stability of the PZT films in biological buffered aqueous solutions by atomic force microscopy, X-ray diffraction and P-E hysteresis loop. In addition, the selectivity of the peptide binding to PZT has been determined by immunofluorescence microscopy and the nature of peptide binding to the PZT surface is probed by X-ray photoemission spectroscopy. INTRODUCTION The use of combinatorial libraries of biological affinity reagents has recently attracted a great deal of interest in materials science as a means to identify novel ligands for binding to a wide range of materials,1 including metals,2 semiconductors,3 complex oxides,4 polymers,5 carbons,6 etc. For example, using the phage display process, short peptide sequences applicable in the synthesis of new nanoparticles7 and the self-assembly of complex nanostructures8 have been identified. To date, however, considerably lesseffort has been directed at determining the binding mechanism of these ligands to their associated materials.9 In prior work, we demonstrated that a constrained heptapeptide sequence, CISLLHSTC (referred to as TAR-1), could selectively associate with the surface of the perovskite ferroelectric, lead zirconium titanate, PZT.4,10 Most importantly, the TAR-1 sequence was found not to bind to other materials commonly encountered in the fabrication of an integrated device (e.g., Au, Pt, SiOx, and a wide variety of organic photoresists), making the TAR-1 sequence an ideal ligand for the successful coupling of biological functional components with lithographically-patterned ferroelectrics. The next step in the successful application of the peptide in coupling functional, genetically engineered biological molecules to PZT is characterization of several materials issues that will be important for the fabrication of a ferroelectric-actuated biomolecular device. First, a sufficiently low surface roughness of the PZT films will be required t
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