Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape

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35 Citations (Scopus)

Abstract

The long-range side-chain repulsion between the (1R,2R,3R,5R)-2-amino-6,6- dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in β-peptide oligomers.

Original languageEnglish
Pages (from-to)177-179
Number of pages3
JournalChemical Communications
Issue number2
DOIs
Publication statusPublished - 2009

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Heptanes
Heptane
Carboxylic Acids
Carboxylic acids
Oligomers
Peptides

ASJC Scopus subject areas

  • Metals and Alloys
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Catalysis
  • Chemistry(all)

Cite this

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title = "Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape",
abstract = "The long-range side-chain repulsion between the (1R,2R,3R,5R)-2-amino-6,6- dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in β-peptide oligomers.",
author = "A. Het{\'e}nyi and Z. Szakonyi and I. M{\'a}ndity and {\'E}va Szolnoki and G. T{\'o}th and T. Martinek and F. F{\"u}l{\"o}p",
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publisher = "Royal Society of Chemistry",
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T1 - Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape

AU - Hetényi, A.

AU - Szakonyi, Z.

AU - Mándity, I.

AU - Szolnoki, Éva

AU - Tóth, G.

AU - Martinek, T.

AU - Fülöp, F.

PY - 2009

Y1 - 2009

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AB - The long-range side-chain repulsion between the (1R,2R,3R,5R)-2-amino-6,6- dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in β-peptide oligomers.

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