Abstract
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 language | English (US) |
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Pages (from-to) | 3963-3966 |
Number of pages | 4 |
Journal | Organic Letters |
Volume | 3 |
Issue number | 24 |
DOIs | |
State | Published - Nov 29 2001 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry