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Chemistry and Industry of Forest Products ›› 2019, Vol. 39 ›› Issue (1): 115-122.doi: 10.3969/j.issn.0253-2417.2019.01.017

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Effect of Metal Ions on Interaction Between Helicid and Bovine Serum Albumin

Dandan ZHAO1,Xiaowei JIN1,Jingnan SHI1,Yuzhen ZHANG1,Hedong BIAN1,2,*(),Yongzhi LIAO2   

  1. 1. School of Chemistry and Chemical Engineering, Guangxi University for Nationalities; Guangxi Key Laboratory of Chemistry and Engineering of Forest Products, Nanning 530006, China
    2. Guangxi Academy of Fishery Sciences, Nanning 530021, China
  • Received:2018-09-30 Online:2019-02-25 Published:2019-03-14
  • Contact: Hedong BIAN E-mail:gxunchem@163.com
  • Supported by:


The effect of Fe3+, Cu2, Ni2+, Zn2+on the interaction reaction between helicid(HLD)and bovine serum albumin(BSA)was investigated by fluorescence spectroscopy under similarity physiological conditions. The results showed that the fluorescence of BSA was quenched via HLD by forming stable complexes. The quenching constants(kq)calculated by Stern-Volmer equation under 293, 298 and 303 K were 6.316, 5.147 and 4.040×1012 L/(mol·s), respectively. The binding constants(K) were 9.10×105, 7.76×105, and 4.97 ×105 L/mol, respectively. The distance between the tryptophan residues of BSA and HLD was 4.79 nm by using Föster′s equation, and it decreased after interaction with metal ions. The theromodynamic parameters indicated that the force between HLD and BSA were hydrogen band and van der Waals forces. The effects of HLD and different metal ions on the secondary structure of BSA were studied using circular dichroism(CD) spectroscopy. The results showed that the addition of HLD changed the conformation of BSA in the binding reaction, and α-helix content decreased. The secondary structure of BSA was also changed by the addition of metal ions and α-helix content further reduced obviously.

Key words: bovine serum albumin, helicid, metal ions, interaction

CLC Number: