Building ß-peptide H10/12 foldamer helices with six-membered cyclic side-chains: fine-tuning of folding and self-assembly.
Org Lett
; 12(23): 5584-7, 2010 Dec 03.
Article
in En
| MEDLINE
| ID: mdl-21050013
ABSTRACT
The ability of the ß-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) residues 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 ~100 nm in diameter.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptides
/
Protein Folding
Language:
En
Journal:
Org Lett
Journal subject:
BIOQUIMICA
Year:
2010
Document type:
Article
Affiliation country:
Hungary