Evidence that the β-peptide 14-helix is stabilized by β3-residues with side-chain branching adjacent to the β-carbon atom

Tami L. Raguse, Jonathan R. Lai, Samuel H. Gellman

Research output: Contribution to journalArticlepeer-review

62 Scopus citations


Oligomers of β-substituted β-amino acids ('β3-peptides') are known to adopt a helical secondary structure defined by 14-membered ring hydrogen bonds ('14-helix'). Here, we describe a deca-β3-peptide, 1, that does not adopt the 14-helical conformation and that may prefer an alternative secondary structure, β3-Peptide 1 is composed exclusively of residues with side chains that are not branched adjacent to the β-C-atom β3-hLeu, β3-hLys, and β3-hTyr). In contrast, an analogous β3-peptide, 2, containing β3-hVal residues in place of the β3-hLeu residues of 1, adopts a 14-helical conformation in MeOH, according to CD data. These results illustrate the importance of side-chain branching in determining the conformational preferences of β3-peptides.

Original languageEnglish (US)
Pages (from-to)4154-4164
Number of pages11
JournalHelvetica Chimica Acta
Issue number12
StatePublished - Dec 1 2002
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Biochemistry
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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