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Peptides with selective affinity for carbon nanotubes

Abstract

Because of their extraordinary electronic and mechanical properties, carbon nanotubes have great potential as materials for applications ranging from molecular electronics to ultrasensitive biosensors. Biological molecules interacting with carbon nanotubes provide them with specific chemical handles that would make several of these applications possible. Here we use phage display to identify peptides with selective affinity for carbon nanotubes. Binding specificity has been confirmed by demonstrating direct attachment of nanotubes to phage and free peptides immobilized on microspheres. Consensus binding sequences show a motif rich in histidine and tryptophan, at specific locations. Our analysis of peptide conformations shows that the binding sequence is flexible and folds into a structure matching the geometry of carbon nanotubes. The hydrophobic structure of the peptide chains suggests that they act as symmetric detergents.

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Figure 1: Electron microscope images.
Figure 2: Change in frequency of occurrence of H, W, F and K with detergent concentration.
Figure 3: Binding affinity measured by the number of plaque-forming units in the binding pool.
Figure 4: Low-energy conformation of sequences.
Figure 5: Factors affecting binding strength.

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Acknowledgements

The work of Y.M.C., E.S.H. and S.Y.C. was supported through a grant from the DuPont–MIT alliance and the Office of Naval Research, Grant No. N00014-01-1-0272.

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Correspondence to Anand Jagota.

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The authors declare no competing financial interests.

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Wang, S., Humphreys, E., Chung, SY. et al. Peptides with selective affinity for carbon nanotubes. Nature Mater 2, 196–200 (2003). https://doi.org/10.1038/nmat833

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