Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues.

Abstract

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.

DOI: 10.1021/ja103233a

3 Figures and Tables

Statistics

050010002011201220132014201520162017
Citations per Year

345 Citations

Semantic Scholar estimates that this publication has 345 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Guo2010HelixFI, title={Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues.}, author={Li Guo and Aaron M. Almeida and Weicheng Zhang and Andrew G Reidenbach and Soo Hyuk Choi and Ilia A. Guzei and Samuel H. Gellman}, journal={Journal of the American Chemical Society}, year={2010}, volume={132 23}, pages={7868-9} }