Ranking the affinity of aromatic residues for carbon nanotubes by using designed surfactant peptides.

@article{Xie2008RankingTA,
  title={Ranking the affinity of aromatic residues for carbon nanotubes by using designed surfactant peptides.},
  author={Hui Xie and Eric J Becraft and Ray H Baughman and Alan B Dalton and Gregg R. Dieckmann},
  journal={Journal of peptide science : an official publication of the European Peptide Society},
  year={2008},
  volume={14 2},
  pages={139-51}
}
A series of surfactant peptides were created to evaluate the affinity of aromatic AAs for single-walled carbon nanotubes in the absence of complications from peptide folding or self-association. Each surfactant peptide has a lipidlike architecture, with two Lys residues at the C-terminus as a hydrophilic head, five Val residues to form a hydrophobic tail, and the testing AA at the N-terminus. Raman and CD spectroscopic studies reveal that the surfactant peptides have a large unordered… CONTINUE READING

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