Journal
ORGANIC LETTERS
Volume 12, Issue 23, Pages 5584-5587Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ol102494m
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Funding
- Hungarian Research Foundation [NK81371]
- COST [CM0803]
- HAS
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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.
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