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Selective Suspension of Single-Walled Carbon Nanotubes Using β-Sheet Polypeptides

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Department of Chemistry, University of Rochester, Rochester, New York 14627, United States
Institute of Optics, University of Rochester, Rochester, New York 14627, United States
*E-mail [email protected]; Ph (585) 275-5093 (T.D.K.).
Cite this: J. Phys. Chem. C 2014, 118, 11, 5935–5944
Publication Date (Web):February 20, 2014
https://doi.org/10.1021/jp410870y
Copyright © 2014 American Chemical Society

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    Abstract

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    Individual single-walled carbon nanotubes (SWNTs) were suspended in water using amphipathic β-sheet peptides of the general sequence Ac-(XKXE)2-NH2. By substituting natural and nonnatural amino acids of varying aromatic and hydrophobic character in the X position, the interactions between the peptide and the nanotube sidewall could be systematically varied. Surprisingly, enhancing the degree of favorable π–π and hydrophobic interactions, which strongly influence the self-assembly properties of these peptides, did not correlate with an improvement in nanotube dispersion efficiency. We found that substituents in the X-position of the peptides play a significant role in SWNT interaction and contributes to (n,m) structure specificity.

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    FT-IR and CD characterization of peptides; chirality distribution for HiPco SWNTs; PLE maps for all peptides; TEM analysis of peptides; representative TEM images of peptide-dispersed SWNTs; HPLC and MALDI-TOF-MS traces for peptide characterization; sample preparation methods for the various surfactants used for comparison. This material is available free of charge via the Internet at http://pubs.acs.org.

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