Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains fine-tuning of folding and self-assembly /
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...
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| Dokumentumtípus: | Cikk |
| Megjelent: |
American Chemical Society
2010
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| Sorozat: | ORGANIC LETTERS
12 No. 23 |
| doi: | 10.1021/ol102494m |
| mtmt: | 1412123 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/11877 |
| Tartalmi kivonat: | 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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| Terjedelem/Fizikai jellemzők: | 5584-5587 |
| ISSN: | 1523-7060 |