A heterocyclic peptide nanotube

J Am Chem Soc. 2003 Aug 6;125(31):9372-6. doi: 10.1021/ja034358h.

Abstract

An open-ended hollow tubular structure is designed based on hydrogen-bond-directed self-assembly of a chimeric cyclic peptide subunit comprised of alternating alpha- and epsilon-amino acids. The design features a novel 1,4-disubstituted-1,2,3-triazole epsilon-amino acid and its utility as a peptide backbone substitute. The N-Fmoc-protected epsilon-amino acid was synthesized in high yield and optical purity in three steps from readily available starting materials and was employed in solid-phase peptide synthesis to afford the desired cyclic peptide structure. The cyclic peptide self-assembly has been studied in solution by (1)H NMR and mass spectrometry and the resulting tubular ensemble characterized in the solid state by X-ray crystallography.

Publication types

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

MeSH terms

  • Amino Acids / chemistry
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Models, Molecular
  • Nanotechnology / methods*
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / chemistry*
  • Protein Conformation
  • Triazoles / chemical synthesis
  • Triazoles / chemistry*

Substances

  • Amino Acids
  • Peptides, Cyclic
  • Triazoles