Effect of electron-donating and electron-withdrawing groups on peptide/single-walled carbon nanotube interactions

被引：0
|
作者：
Poenitzsch, Vasiliki Z. [1 ]
Winters, David C. [1 ]
Xie, Hui [2 ]
Dieckmann, Gregg R. [1 ,2 ]
Dalton, Alan B. [3 ]
Musselman, Inga H. [1 ,2 ]
机构：
[1] Department of Chemistry, University of Texas at Dallas, Richardson, TX 75080, United States
[2] Alan G. MacDiarmid NanoTech Institute, University of Texas at Dallas, 800 West Campbell Road, Richardson, TX 75080, United States
[3] Department of Physics, University of Surrey, Guildford GU2 7XH, United Kingdom
来源：
Journal of the American Chemical Society | 2007年 / 129卷 / 47期
关键词：
Nano-1; a designed peptide; has been demonstrated to efficiently disperse individual single-walled carbon nanotubes (SWNTs) by folding into an amphiphilic α-helix wherein the phenylalanine (Phe) residues on the hydrophobic face of the helix interact via π-stacking with the aromatic surface of the SWNT. In this study; the ability of electron-donating (hydroxyl) and electron-withdrawing (nitro) groups on the phenyl ring of Phe to affect the interactions between the peptide and SWNTs is examined by substituting the Phe residues in the nano-1 sequence with tyrosine and p-nitro-phenylalanine; respectively. Atomic force microscopy measurements and optical absorption spectroscopy revealed that the ability to disperse individual SWNTs increases with increasing electron density of the aromatic residue on the hydrophobic face of the amphiphilic helical peptides. Scanning tunneling spectroscopy (STS) and Raman analyses were used to examine the effect of noncovalent protein functionalization on the electronic properties of SWNTs. Small shifts in the Raman G band peak for the peptide/SWNT composites; as well as weak features that appear near the Fermi energy (Ef) in the STS dI/dV spectra of the peptide-coated SWNTs; are suggestive of a weak charge-transfer interaction between the peptides and the SWNTs. © 2007 American Chemical Society;
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页码：14724 / 14732
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