Difference in self-assembling morphology of peptide nanorings

Hajime Okamoto*, Tetsuo Yamada, Hiroshi Miyazaki, Tsutomu Nakanishi, Kyozaburo Takeda, Kenji Usui, Ikuo Obataya, Hisakazu Mhara, Hiroaki Azehara, Wataru Mizutani, Katsushi Hashimoto, Hiroshi Yamaguchi, Yoshiro Hirayama

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


We synthesized the peptide nanorings of cyclo[-(D-Ala-L-Gln)3], cyclo[-(D-Cys-L-Gln)3], cyclo[-D-Cys-L-His-D-Ala-L-Asn-Gly-L-Gln-] and cyclo[-(L-Gln)3], and studied the way in which the difference in the type and/or number of component amino acid residues changes the self-assembling morphology of the nanorings on gold substrates by atomic force microscopy. The study revealed that cyclo[-(D-Ala-L-Gln)3] formed nanotube bundles through inter-ring hydrogen bonds, while the nanorings of cyclo[-(D-Cys-L-Gln)3] adhered to the gold surface directly due to the high affinity of thiol to gold. In contrast, a random amino acid sequence of cyclo[-D-Cys-L-His-D-Ala-L-Asn-Gly-L-Gln-] resulted in many isolated nanotubes, which were first observed in the present study. While the D,L-peptide nanotubes have very straight forms, the homo-L-peptide of cyclo[-(L-Gln)5] formed interesting randomly branching nanotubes that were entwined and grew on the substrate. Scanning tunneling microscopy was also performed and high-resolution images of both the peptide nanotubes and the nanotube bundles were obtained.

Original languageEnglish
Pages (from-to)8240-8248
Number of pages9
JournalJapanese Journal of Applied Physics, Part 1: Regular Papers and Short Notes and Review Papers
Issue number11
Publication statusPublished - 2005 Nov 9


  • Atomic force microscopy
  • Cyclic peptide
  • Nanotube
  • Scanning tunneling microscopy
  • Self-assembly, synthesis

ASJC Scopus subject areas

  • General Engineering
  • General Physics and Astronomy


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