Toward beta-peptide tertiary structure: self-association of an amphiphilic 14-helix in aqueous solution.
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]
Raguse
T L
TL
Department of Chemistry, Graduate Program in Biophysics, University of Wisconsin, Madison, WI 53706, USA.
Lai
J R
JR
LePlae
P R
PR
Gellman
S H
SH
D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions; D014867:Water / Q000737:chemistry
D010455:Peptides; D012996:Solutions; D014867:Water