Chem. J. Chinese Universities ›› 2010, Vol. 31 ›› Issue (8): 1529.

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Interaction Between Berberine and Human Gamma Globulin in Membrane Mimetic Environments

LI Ying1*, WANG Chao1, HU Zhi-De2   

  1. 1. Key Laboratory of Integrated Regulation and Resource Development on Shallow Lakes, Ministry of Education, College of Environment,    Hohai University, Nanjing  210098,  China;
    2. College of Chemistry and Chemical Engineering,  Lanzhou University, Lanzhou 730000,  China
  • Received:2009-11-04 Online:2010-08-10 Published:2010-08-10
  • Contact: LI Ying. E-mail: hj6688@hhu.edu.cn
  • Supported by:

    教育部重点实验室开放基金(批准号: 2007KJ002)和中央高校基本科研业务费专项资金(批准号: B1020182)资助.

Abstract: The interaction between berberine and human gamma globulin(HGG) in AOT/ isoctant/water reverse micellar was studied by fluorescence quenching technique, UV absorption spectroscopy, circular dischroism(CD) spectroscopy and dynamic light scattering(DLS) technique. The interaction of HGG with berberine at 289, 296, 303 and 310 K in water-surfactant molar ratio(ω0=25) reverse micellar was characterized by one binding site with the affinity constant K at 4.50×104, 4.18×104, 4.13×104 and 3.76×104 L/mol, respectively. The affinities in reverse micellar were much higher than that in buffer solution. The CD spectra results proved that the protein secondary structure changed in the reverse micellar in the absence and presence of berberine compared with the free form of HGG in buffer. The binding process was exothermic and spontaneous, as indicated by the thermodynamic analyses. The results show that hydrophobic and electrostatic interaction play the main roles in the binding of berberine to HGG. Furthermore, the DLS data suggested that HGG may locate inside of the reverse micellar and berberine could interact with them.

Key words: Berberine, Human gamma globulin, Interaction

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