01534nab a2200265 i 4500 publ11877 20200225094116.0 170831s2010 hu o 0|| zxx d 1523-7060 10.1021/ol102494m doi 1412123 mtmt SZTE Publicatio Repozitórium hun zxx Mándity István M. Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains [elektronikus dokumentum] : fine-tuning of folding and self-assembly / Mándity István M. American Chemical Society 2010 5584-5587 ORGANIC LETTERS 12 No. 23 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. Fülöp Lívia aut Vass Elemér aut Tóth Gábor aut Martinek Tamás A. aut Fülöp Ferenc aut http://publicatio.bibl.u-szeged.hu/11877/1/mandity2010.pdf Dokumentum-elérés