Building beta-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly

作者：Mandity Istvan M; Fueloep Livia; Vass Elemer; Toth Gabor K; Martinek Tamas A^*; Fueloep Ferenc

来源：Organic Letters, 2010, 12(23): 5584-5587.

DOI：10.1021/ol102494m

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.

• 出版日期2010-12-3