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.