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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Bibliographic Details
Main Authors: Mándity István M.
Fülöp Lívia
Vass Elemér
Tóth Gábor
Martinek Tamás A.
Fülöp Ferenc
Format: Article
Published: American Chemical Society 2010
Series:ORGANIC LETTERS 12 No. 23
doi:10.1021/ol102494m

mtmt:1412123
Online Access:http://publicatio.bibl.u-szeged.hu/11877
Description
Summary: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.
Physical Description:5584-5587
ISSN:1523-7060