Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (7): 1337.

• Articles • Previous Articles     Next Articles

Self-assembling Structure and Mechanism of a Wedge-shaped Peptide Detergent A3V3D

CHEN Yong-Zhu, QIU Feng, ZHAO Xiao-Jun*   

  1. Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital, Sichuan University, Chengdu 610041, China
  • Received:2008-12-10 Online:2009-07-10 Published:2009-07-10
  • Contact: ZHAO Xiao-Jun. E-mail: xiaojunz@mit.edu
  • Supported by:

    国家自然科学基金(批准号: 50775152)资助.

Abstract:

A wedge-shaped peptide detergent A3V3D was designed by changing the amino acid sequence of traditional peptide detergents. Although the secondary structure of this peptide is random coil as revealed by circular dichroism(CD) assessment, it can still undergo well-ordered self-assemble in water solution into stable, smooth and straight nanofibers, which are observed by transmission electron microscopy(TEM) and atomic force microscopy(AFM). Pyrene probe fluorescence analysis indicated that it could form hydrophobic domains in which pyrene molecules were imbedded. It was believed that driven by its wedge-like geometrical shape, A3V3D undergoes self-assemble in the form of cylindrical micelles, making it a novel self-assembling peptide material, and indicating the critical role of geometrical shape effect in controlling the self-assembling behavior.

Key words: Self-assembly; Peptide detergent; Geometrical shape effect; Nanofiber

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