Structural and Electronic Properties of Ordered Peptide Assemblies on Gold

Researchers:
Scott Reed
Rob Gilbertson
 A more complete understanding of the effect of peptide composition on electron transfer rates in organized biomolecule assemblies is necessary to understand complex biological systems and to design electronic biomaterials. To investigate the details of polypeptide-mediated electron transfer, we prepared and characterized the first highly ordered peptide assemblies on an electrode surface. To probe the stabilizing influence of hydrogen bonding within a monolayer assembly and to further understand the electron transfer properties of polypeptides, we have now investigated a family of 2-D peptide assemblies. In all cases, strong interchain hydrogen bonding serves to cross-link and stabilize the monolayers.

We recently found that some peptide monolayers facilitate electron transfer to a greater extent than all-hydrocarbon monolayers. This unique system is being used to quantitatively investigate electron transfer kinetics in peptide materials and to explore their use as highly stable foundations for the assembly of nanostructures and sensors.

Recent publications.

Clegg, R. S.; Hutchison, J. E. "Hydrogen-Bonding, Self-Assembled Monolayers: Ordered Molecular Films for Study of Through-Peptide Electron Transfer," Langmuir 1996, 12, 5239.

Clegg, R. S.; Reed, S. M.; Hutchison, J. E. "Self-Assembled Monolayers Stabilized by Three-Dimensional Networks of Hydrogen Bonds," J. Am. Chem. Soc. 1998, 120, 2486-2487.

Clegg, R. S.; Hutchison, J. E. "Self-Assembled Monolayers with Internal Amides: Control of Assembly Structures by Hydrogen Bonding Instead of Monolayer–Substrate Epitaxy." J. Am. Chem. Soc. 1999, in press.

Clegg, R. S.; Reed, S. M.; Smith, R. K.; Barron, B. L.; Rear, J. A.; Hutchison, J. E. "The Interplay of Lateral and Tiered Interactions in Stratified Self-Organized

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