Characteristic structural parameters for the γ-peptide 14-helix: importance of subunit preorganization

Angew Chem Int Ed Engl. 2011 Jun 20;50(26):5843-6. doi: 10.1002/anie.201101301. Epub 2011 May 12.

Abstract

We report crystallographic data for a set of homologous γ-peptides that contain a Boc-protected residue derived from the flexible gabapentin monomer at the N-terminus and cyclically constrained γ-residues at all other positions. The crystallized γ-peptides range in length from 3 to 7 residues. Previously only one atomic-resolution structure had been available for a short γ-peptide 14-helix. The new data provided here allow derivation of characteristic parameters for the γ-peptide 14-helix, and establish guidelines for characterizing 14-helical folding in solution via 2D NMR. In addition, the results suggest that the substitution pattern of a γ-residue has a profound effect on the propensity for 14-helical folding.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amines / chemistry
  • Crystallography, X-Ray
  • Cyclohexanecarboxylic Acids / chemistry
  • Gabapentin
  • Hydrogen Bonding
  • Peptides / chemistry*
  • Protein Structure, Secondary
  • gamma-Aminobutyric Acid / chemistry

Substances

  • Amines
  • Cyclohexanecarboxylic Acids
  • Peptides
  • gamma-Aminobutyric Acid
  • Gabapentin