Use of designed amphiphilic peptides for the solubilization, separation and self-assembly of carbon nanotubes

I&EC 186

Alfonso Ortiz-Acevedo1, Alan B. Dalton2, Vasiliki Zorbas1, Ray H. Baughman3, Rockford K. Draper4, Inga H. Musselman1, and Gregg R. Dieckmann1. (1) Department of Chemistry, The University of Texas at Dallas, 2601 North Floyd Road, Richardson, TX 75083-0688, (2) NanoTech Institute, University of Texas at Dallas, 2601 North Floyd Road, Richardson, TX 75083-0688, (3) Departments of Chemistry and Physics and the Nanotech Institute, University of Texas at Dallas, 2601 North Floyd Road, Richardson, TX 75083-0688, (4) Departments of Molecular and Cell Biology and Chemistry, University of Texas at Dallas, 2601 North Floyd Road, Richardson, TX 75083-0688
Utilizing de novo protein design strategies, we have created a family of amphiphilic peptides that bind noncovalently to single-walled carbon nanotubes. This noncovalent functionalization of the nanotubes leads to solubilization in aqueous solution, nanotube debundling, and concomitant self assembly of the peptide-wrapped nanotubes into several different macromolecular architectures depending on solution conditions. This poster will present details of the peptide design, as well as the characterization of the peptides and the peptide/nanotube composites using circular dichroism, electron microscopy and Raman spectroscopy.
 

Industrial and Engineering Chemistry Posters
5:00 PM-7:00 PM, Tuesday, March 30, 2004 Anaheim Convention Center -- Hall A, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, March 29, 2004 Anaheim Convention Center -- Hall A, Sci-Mix

Division of Industrial and Engineering Chemistry

The 227th ACS National Meeting, Anaheim, CA, March 28-April 1, 2004