Remarkable stabilization of the α-helix structure by an intramolecular host-guest bridge in a cyclodextrin-peptide hybrid

Keita Hamasaki, Ryosuke Suzuki, Hisakazu Mihara, Akihiko Ueno

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A cyclodextrin-peptide hybrid (CD-peptide) bearing three units of γ-cyclodextrin, cholic acid, and a dansyl fluorophore in the side chain has been prepared. In this novel CD-peptide, the cholic acid unit acts as an internal guest and forms an intramolecular inclusion complex with γ-cyclodextrin in the CD-peptide. This intramolecular complex works as a host-guest bridge in the CD-peptide and remarkably stabilizes the α-helix structure of the CD-peptide.

Original languageEnglish
Pages (from-to)262-265
Number of pages4
JournalMacromolecular Rapid Communications
Volume22
Issue number4
DOIs
Publication statusPublished - 2001 Feb 28
Externally publishedYes

Fingerprint

Cyclodextrins
Peptides
Stabilization
Cholic Acid
Bearings (structural)
Acids
Fluorophores

ASJC Scopus subject areas

  • Polymers and Plastics
  • Materials Chemistry

Cite this

Remarkable stabilization of the α-helix structure by an intramolecular host-guest bridge in a cyclodextrin-peptide hybrid. / Hamasaki, Keita; Suzuki, Ryosuke; Mihara, Hisakazu; Ueno, Akihiko.

In: Macromolecular Rapid Communications, Vol. 22, No. 4, 28.02.2001, p. 262-265.

Research output: Contribution to journalArticle

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