Toward β-Peptide Tertiary Structure: Self-Association of an Amphiphilic 14-Helix in Aqueous Solution
Organic Letters2001Vol. 3(24), pp. 3963–3966
Citations Over TimeTop 10% of 2001 papers
Abstract
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 beta-peptide realm by showing that a 10-residue beta-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. [structure: see text]
Related Papers
- → Macrocycles of Higher Ortho-Phenylenes: Assembly and Folding(2019)6 cited
- → Synthesis and structural characterisation as 12-helix of the hexamer of a β-amino acid tethered to a pyrrolidin-2-one ring(2006)16 cited
- → Macrocycles of Higher Ortho-Phenylenes: Assembly and Folding(2019)1 cited
- → Quaternary structure of human nucleoside diphosphate kinase isoforms HA and HB in solution(1996)10 cited
- → Macrocycles of Higher ortho-Phenylenes: Assembly and Folding(2019)