Gamma4-aminoxy peptides as new peptidomimetic foldamers

J Am Chem Soc. 2004 Dec 15;126(49):15980-1. doi: 10.1021/ja044493+.

Abstract

The conformational properties of peptides 1-3 of gamma-aminoxy acids have been investigated by using FT-IR, NMR spectroscopy, and X-ray crystallography. Diamide 1 consisting of unsubstituted gamma-aminoxy acid cannot form intramolecular hydrogen bond. A novel gamma N-O turn involving a 10-membered-ring intramolecular hydrogen bond between NHi+2 and COi is formed in gamma4-aminoxy peptides 2 and 3. Triamides 3 prefers a new helical structure featuring two consecutive gamma N-O turns. Therefore, gamma4-aminoxy peptides represent new peptidomimetic foldamers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Biomimetic Materials / chemistry
  • Circular Dichroism
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides / chemistry*
  • Protein Folding
  • Protein Structure, Secondary
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Amino Acids
  • Peptides