Importance of aromatic content for peptide/single-walled carbon nanotube interactions.
We have previously demonstrated that a designed amphiphilic peptide helix, denoted nano-1, coats and debundles single-walled carbon nanotubes (SWNTs) and promotes the assembly of these coated SWNTs into novel hierarchical structures via peptide-peptide interactions. The purpose of this study is to better understand how aromatic content impacts interactions between peptides and SWNTs. We have designed a series of peptides, based on the nano-1 sequence, in which the aromatic content is systematically varied. Atomic force microscopy measurements and optical absorption spectroscopy reveal that the ability to disperse individual SWNTs increases with increasing aromatic residues in the peptide. Altogether, the results indicate that pi-stacking interactions play an important role in peptide dispersion of SWNTs.
Zorbas
Vasiliki
V
Department of Chemistry, NanoTech Institute, and Department of Molecular and Cell Biology, The University of Texas at Dallas, 2601 North Floyd Road, Richardson, Texas 75080, USA.
Smith
Amy L
AL
Xie
Hui
H
Ortiz-Acevedo
Alfonso
A
Dalton
Alan B
AB
Dieckmann
Gregg R
GR
Draper
Rockford K
RK
Baughman
Ray H
RH
Musselman
Inga H
IH
D006841:Hydrocarbons, Aromatic / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D036103:Nanotechnology / Q000379:methods*; D037742:Nanotubes, Carbon / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis
D006841:Hydrocarbons, Aromatic; D037742:Nanotubes, Carbon; D010455:Peptides