Toward β-peptide tertiary structure: Self-association of an amphiphilic 14-helix in aqueous solution

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

Research output: Contribution to journalArticle

112 Scopus citations


equation presented A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the β-peptide realm by showing that a 10-residue β-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range.

Original languageEnglish (US)
Pages (from-to)3963-3966
Number of pages4
JournalOrganic Letters
Issue number24
StatePublished - Nov 29 2001
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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