Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains: Fine-tuning of folding and self-assembly

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Abstract

The ability of the β-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.

Original languageEnglish
Pages (from-to)5584-5587
Number of pages4
JournalOrganic Letters
Volume12
Issue number23
DOIs
Publication statusPublished - Dec 3 2010

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Carboxylic Acids
Polymorphism
helices
Self assembly
folding
peptides
Conformations
self assembly
Tuning
tuning
Peptides
polymorphism
carboxylic acids
rings
configurations

ASJC Scopus subject areas

  • Organic Chemistry
  • Physical and Theoretical Chemistry
  • Biochemistry

Cite this

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title = "Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains: Fine-tuning of folding and self-assembly",
abstract = "The ability of the β-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.",
author = "I. M{\'a}ndity and L. F{\"u}l{\"o}p and E. Vass and G. T{\'o}th and T. Martinek and F. F{\"u}l{\"o}p",
year = "2010",
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T1 - Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains

T2 - Fine-tuning of folding and self-assembly

AU - Mándity, I.

AU - Fülöp, L.

AU - Vass, E.

AU - Tóth, G.

AU - Martinek, T.

AU - Fülöp, F.

PY - 2010/12/3

Y1 - 2010/12/3

N2 - The ability of the β-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.

AB - The ability of the β-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.

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