Chem. J. Chinese Universities

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Supramolecular Monitoring and the Related Mechanism of Aggregation/Disaggregation of Melittin in Different Media

WANG Lei1, HAO Ya-Qiong1, LI Yue1, LI Zheng-Qiang3, WU Yu-Qing1,2*   

    1. State Key Laboratory for Supramolecular Structure and Materials, Jilin University, Changchun 130012, China;
    2. Key Laboratory of Molecular Engineering of Polymers of Ministry of Education, Fudan University, Shanghai 200433, China;
    3. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130021, China
  • Received:2007-10-09 Revised:1900-01-01 Online:2008-06-10 Published:2008-06-10
  • Contact: WU Yu-Qing

Abstract: Melittin, with strong pharmacological effects and biological activity, is the major component of bee venom. The physiological function of melittin depends upon its secondary structure and aggregation state due to which the peptide loses its activity. Once the aggregation/disaggregation processes can be effectively monitored, it will lay the foundation for clinical applications by exploring its function and mechanism. In this paper the aggregation/disaggregation processes were explored, the related mechanism and the α-helix content of melittin in aqueous solution is controlled by 2-hydroxypropyl-β-cyclodextrin, sodium chloride or 1,2-dioleoyl-sn-glycero-3-phosphocholine(DOPC) through fluorescence spectra and circular dichroism(CD).

Key words: Melittin, 2-Hydroxypropyl-β-cyclodextrin, NaCl, 1,2-Dioleoyl-sn-glycero-3-phosphocholine(DOPC), α-Helix

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