Controlled assembly of carbon nanotubes by designed amphiphilic Peptide helices.
Carbon nanotubes have properties potentially useful in diverse electrical and mechanical nanoscale devices and for making strong, light materials. However, carbon nanotubes are difficult to solubilize and organize into architectures necessary for many applications. In the present paper, we describe an amphiphilic alpha-helical peptide specifically designed not only to coat and solubilize carbon nanotubes, but also to control the assembly of the peptide-coated nanotubes into macromolecular structures through peptide-peptide interactions between adjacent peptide-wrapped nanotubes. The data presented herein show that the peptide folds into an amphiphilic alpha-helix in the presence of carbon nanotubes and disperses them in aqueous solution by noncovalent interactions with the nanotube surface. Electron microscopy and polarized Raman studies reveal that the peptide-coated nanotubes assemble into fibers with the nanotubes aligned along the fiber axis. Most importantly, the size and morphology of the fibers can be controlled by manipulating solution conditions that affect peptide-peptide interactions.
Dieckmann
Gregg R
GR
Department of Chemistry, The University of Texas at Dallas, 2601 North Floyd Road, Richardson, Texas 75083-0688, USA. dieckgr@utdallas.edu
Dalton
Alan B
AB
Johnson
Paul A
PA
Razal
Joselito
J
Chen
Jian
J
Giordano
Geoff M
GM
Muñoz
Edgar
E
Musselman
Inga H
IH
Baughman
Ray H
RH
Draper
Rockford K
RK
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D017348:Microscopy, Electron, Scanning Transmission; D008958:Models, Molecular; D008969:Molecular Sequence Data; D036103:Nanotechnology / Q000379:methods; D037742:Nanotubes, Carbon / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman
D037742:Nanotubes, Carbon; D010455:Peptides