Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues.
We report the first high-resolution structural data for the beta/gamma-peptide 13-helix (i,i+3 C=O...H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of beta- and gamma-amino acid residues. Our characterization includes both crystallographic and 2D NMR data. Previous studies suggested that beta/gamma-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized beta- and gamma-residues, which strongly promote 13-helical folding by the 1:1 beta/gamma backbone.
Guo
Li
L
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Almeida
Aaron M
AM
Zhang
Weicheng
W
Reidenbach
Andrew G
AG
Choi
Soo Hyuk
SH
Guzei
Ilia A
IA
Gellman
Samuel H
SH
D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012996:Solutions
D000596:Amino Acids; D010455:Peptides; D012996:Solutions