A heterocyclic peptide nanotube.
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.
Horne
W Seth
WS
Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.
Stout
C David
CD
Ghadiri
M Reza
MR
D000596:Amino Acids / Q000737:chemistry; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D036103:Nanotechnology / Q000379:methods*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D014230:Triazoles / Q000138:chemical synthesis / Q000737:chemistry*
D000596:Amino Acids; D010456:Peptides, Cyclic; D014230:Triazoles