Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones.

@article{Cho2014StabilizationO,
  title={Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones.},
  author={Joonil Cho and Kyohei Sawaki and Shinya Hanashima and Yoshiki Yamaguchi and Motoo Shiro and Kazuhiko Saigo and Yasuhiro Ishida},
  journal={Chemical communications},
  year={2014},
  volume={50 69},
  pages={9855-8}
}
The 14-helix structure of oligo-β-peptides was significantly stabilized by direct attachment of CF3 groups to their backbones. Our studies indicate that this stabilization originates from the CF3-promoted increase in the intramolecular hydrogen-bonding ability of their backbone amides, leading to a novel strategy to stabilize peptide folding.