Theoretical prediction and atomic force microscope observations of the protein nanotube consisting of homo-L-amino acid penta-peptide nanorings

Hajime Okamoto*, Tsutomi Nakanishi, Yukiko Nagai, Kyozaburo Takeda, Ikuo Obataya, Hisakazu Mihara, Hiroaki Azehara, Wataru Mizutani

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

An unusual penta-peptide nanotube was synthesized by a solid-phase method using Fmoc chemistry. This nanotube consists of the natural homo-L-amino acid sequence (cyclo[-(L-Gln)5]), which is different from the already-known DL-peptide nanotubes having an even number of residues. We also observed the morphology by atomic force microscope (AFM) and found meandering tubular structures on the substrate. This result is consistent with our ab initio energy calculations, which show that the penta-peptide nanorings stabilize by breaking the C5 symmetry and stack themselves to form a meandering nanotube through the inter-ring hydrogen bonds.

Original languageEnglish
Pages (from-to)676-679
Number of pages4
JournalJapanese Journal of Applied Physics, Part 1: Regular Papers and Short Notes and Review Papers
Volume42
Issue number2 A
DOIs
Publication statusPublished - 2003 Feb

Keywords

  • AFM observations
  • Ab initio calculations
  • Amino acid
  • Cyclic peptide
  • Peptide synthesis
  • Protein nanotube

ASJC Scopus subject areas

  • Engineering(all)
  • Physics and Astronomy(all)

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