Self-assembly of nanofiber with uniform width from wheel-type trigonal-β-sheet-forming peptide

Kazuya Murasato, Kazunori Matsuura, Nobuo Kimizuka

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

A novel C3 symmetric peptide:conjugate "Wheel-FKFE" consisting of three β-sheet-forming peptides with wheel-like arrangement is developed, and the morphology of self-assembled peptide conjugates in aqueous solutions is observed at various pH. The CD spectra of Wheel-FKFE show the formation of β-sheet structures in pH 6.9 phosphate buffer, whereas random structures are formed in aqueous HCI (pH 3.3) and NaOH (pH 11) solutions. In transmission electron microscopy, nanofibers with a uniform width of 3-4 nm and lengths of several micrometers are observed in pH 6.9 phosphate buffer, whereas nanorods with the width of several nanometers and the length of several tens of nanometers; are observed for that of aqueous HCI (pH 3.3) and NaOH (pH 11) solutions. The uniform width (3-4 nm) of the fibers observed in neutral solution indicates formation of columnar self-assembly of Wheel-FKFEs. The fluorescence spectrum of polarity sensitive dye, sodium 8-anilino-l-naphthalenesulfonate (ANS), in the presence of Wbeel-FKFE fibers revealed that the polarity inside the fibers corresponds to that of acetone, indicating that the internal space of the fibers possesses medium hydrophobic environment.

Original languageEnglish
Pages (from-to)913-918
Number of pages6
JournalBiomacromolecules
Volume9
Issue number3
DOIs
Publication statusPublished - Mar 1 2008

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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