Design and synthesis of 3α-helix peptides forming a cavity for a fluorescent ligand

Ikuo Obataya, Seiji Sakamoto, Akihiko Ueno, Hisakazu Mihara

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


As a model of receptor protein, a series of 3α-helix bundle peptides constructed on a template peptide were designed so as to possess a hydrophobic cavity. The size of cavity was modulated by simple replacements of Leu residues to Ala residues in the hydrophobic core. Binding abilities to 8-anilino-1-naphthalenesulfonic acid (ANS) were estimated by the increase of fluorescence intensity. The peptide having three or four Ala residues in the hydrophobic core remarkably increased the binding ability for ANS, though the peptide having two Ala residues gave an inefficient cavity for ANS. The peptide having six Ala residues decreased the binding ability due to crucial destabilization of the helix bundle structure. This scaffold can be utilized to a receptor model, while further tuning of the sequence is necessary.

Original languageEnglish
Pages (from-to)65-71
Number of pages7
Issue number2
Publication statusPublished - 2001 Jul 16


  • 8-anilino-1-naphthalenesulfonic acid
  • De novo design
  • Peptide
  • Receptor
  • Template-assembled synthetic protein
  • α-helix

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry


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