@article{448,
  author = {István Mándity and L. Fulop and E. Vass and G. Toth and Tamás Martinek and Ferenc Fülöp},
  title = {Building beta-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly},
  abstract = {The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter.},
  journal = {Organic Letters},
  volume = {12},
  number = {23},
  pages = {5584–5587},
  address = {APPELLA DH, 1996, J AM CHEM SOC, V118, P13071},
  issn = {1523-7060},
}