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A heterocyclic peptide nanotube

Academic Article
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Overview

related to degree

  • Horne, William Seth, Ph.D. in Chemistry, Scripps Research 2000 - 2005

authors

  • Horne, William Seth
  • Stout, C. David
  • Ghadiri, M. Reza

publication date

  • August 2003

journal

  • Journal of the American Chemical Society  Journal

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.

subject areas

  • Amino Acids
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Models, Molecular
  • Nanotechnology
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides, Cyclic
  • Protein Conformation
  • Triazoles
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja034358h

PubMed ID

  • 12889966
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Additional Document Info

start page

  • 9372

end page

  • 9376

volume

  • 125

issue

  • 31

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