New helical foldamers: heterogeneous backbones with 1:2 and 2:1 alpha:beta-amino acid residue patterns.
Foldamers, oligomers with strong folding propensities, are subjects of growing interest because such compounds offer unique scaffolds for the development of molecular function. We report two new foldamer classes, oligopeptides with regular 1:2 or 2:1 patterns of alpha- and beta-amino acid residues. Two distinct helical conformations are detected via 2D NMR in methanol for each backbone. One of the helices for each backbone is characterized via X-ray crystallography.
Schmitt
Margaret A
MA
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Choi
Soo Hyuk
SH
Guzei
Ilia A
IA
Gellman
Samuel H
SH
D000596:Amino Acids / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D000596:Amino Acids; D010455:Peptides