1.
Org Lett
; 3(24): 3963-6, 2001 Nov 29.
Article
in English
| MEDLINE
| ID: mdl-11720580
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]
Subject(s)
Peptides/chemistry , Nuclear Magnetic Resonance, Biomolecular , Protein Structure, Secondary , Solutions , Water/chemistry
2.
J Org Chem
; 65(15): 4766-9, 2000 Jul 28.
Article
in English
| MEDLINE
| ID: mdl-10959893