Abstract

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.

Keywords

Carbon nanotubePeptideAmphiphileChemistryNanotubeNanotechnologyMacromoleculeCarbon nanobudRaman spectroscopyHelix (gastropod)Selective chemistry of single-walled nanotubesMaterials scienceOptical properties of carbon nanotubesOrganic chemistryPolymerCopolymerBiochemistry

MeSH Terms

Amino Acid SequenceCircular DichroismMicroscopyElectronScanning TransmissionModelsMolecularMolecular Sequence DataNanotechnologyNanotubesCarbonPeptidesProtein StructureSecondarySpectrum AnalysisRaman

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Publication Info

Year
2003
Type
article
Volume
125
Issue
7
Pages
1770-1777
Citations
487
Access
Closed

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487
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3
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451
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Cite This

Gregg R. Dieckmann, Alan Β. Dalton, Paul A. Johnson et al. (2003). Controlled Assembly of Carbon Nanotubes by Designed Amphiphilic Peptide Helices. Journal of the American Chemical Society , 125 (7) , 1770-1777. https://doi.org/10.1021/ja029084x

Identifiers

DOI
10.1021/ja029084x
PMID
12580602

Data Quality

Data completeness: 81%