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

Research output: Article

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 - jan. 5 2009

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ASJC Scopus subject areas

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

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