Chem. J. Chinese Universities ›› 2011, Vol. 32 ›› Issue (8): 1774.

• Articles • Previous Articles     Next Articles

Self-assembly and Mechanism of Surfactant-like  Peptide A6KA6K

MA Xin1, MENG Qing-Bin2,3, KOU Ying-Ying2, LIANG Yuan-Jun2, GUO Lei2, NI Cai-Hua1*, LIU Ke-Liang2*   

  1. 1.  School of Chemical and Material Engineering, Jiangnan University, Wuxi 214122, China;
    2.    Institute of Pharmacology and Toxicology, Academy of Military Medical Science,  Beijing 100850, China;
    3.   School of Pharmaceutical Sciences, Peking University, Beijing 100191, China
  • Received:2010-10-14 Revised:2010-12-02 Online:2011-08-10 Published:2011-07-19
  • Contact: LIU Ke-Liang;NI Cai-Hua E-mail:keliangliu@yahoo.com;nicaihua2000@163.com
  • Supported by:

    国家重大新药创制科技重大专项(批准号:  2009ZX09301-002, 2009ZX09503-015)资助.

Abstract: A diploid A6KA6K of surfactant-like peptide A6K was designed to study the influence on the length and ratio of the hydrophilic and hydrophobic segments in the peptide self-assembly. The secondary structure of the A6KA6K was mainly random coil and minor α-helix, which characterized by circular dichroism. The results observed by transmission electron microscopy and dynamic light scattering revealed that the peptide could self-assemble to form nanovesicles in aqueous solution. Pyrene probe fluorescence analysis indicated this peptide could form hydrophobic domains in which pyrene molecules were imbedded and undergo self-assembly in the form of micelles. The critical micelle concentration of the peptide was also calculated. Compared with the surfactant peptide A6K reported previously, the longer peptide A6KA6K containing 14 amino acids could formed nanovesicles through self-assembly, because the introduction of a hydrophilic amino acid into the hydrophobic segment of the peptide influenced the hydrophobic interaction of the peptide.

Key words: Surfactant-like peptide, Self-assembly, Fluorescence probe, Nanovesicle

CLC Number: 

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