Gamma4-aminoxy peptides as new peptidomimetic foldamers.
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.
Chen
Fei
F
Department of Chemistry, The University of Hong Kong, Pokfulam Road, Pokfulam, Hong Kong, China.
Zhu
Nian-Yong
NY
Yang
Dan
D
D000596:Amino Acids / Q000737:chemistry*; D040761:Biomimetic Materials / Q000737:chemistry; D002942:Circular Dichroism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
D000596:Amino Acids; D010455:Peptides