Study on Interaction between Coomassie Brilliant Blue G-250 and Bovine Serum Albumin by Fluorescence Spectroscopy and Molecular Modeling
文献类型： 外文期刊
作者：
Wang Yong-gang
1
;
Yang Guang-rui
1
;
Ma Xue-qing
2
;
Leng Fei-fan
1
;
Ma Jian-zhong
1
;
Wang Xiao-li
3
;
作者机构： 1.Lanzhou Univ Technol, Sch Life Sci & Engn, Lanzhou 730050, Gansu, Peoples R China
2.Chinese Acad Agr Sci, State Key Lab Vet Etiol Biol, Natl Foot & Mouth Dis Reference Lab, Lanzhou Vet Res Inst, Lanzhou 730046, Gansu, Peoples R China
3.Chinese Acad Agr Sci, Lanzhou Inst Husb & Pharmaceut Sci, Lanzhou 730050, Gansu, Peoples R China
关键词： Spectroscopy;Molecular modeling;Coomassie brilliant blue G-250;Bovine serum albumin;Interaction
期刊名称：SPECTROSCOPY AND SPECTRAL ANALYSIS （ 影响因子：0.589； 五年影响因子：0.504 ）
ISSN： 1000-0593
年卷期： 2017 年 37 卷 8 期
页码：
收录情况： SCI
摘要： The interaction of coomassie brilliant blue G-250 (CBBG-250) with bovine serum albumin (BSA) was investigated by the methods of fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD). Fluorescence data showed that the quenching of BSA by CBBG-250 was result of forming the complex of BSA-CBBG-250, and CBBG-250 effectively quenched the intrinsic fluorescence of BSA via static quenching. According to Stern-Volmer equation, the binding parameters between CBBG-250 and BSA were determined. The enthalpy change (Delta H) and entropy change (Delta S) were calculated to be -4.38 kJ . mol(-1) and -6.16 J . mol(-1) . K-1, indicating that the hydrogen bonds and hydrophobic interactions played a dominant role in the binding. The conformational investigation revealed the alpha-helical structure was decreased and the polypeptides of BSA were slightly folded with the addition of CBBG-250 by synchronous fluorescence. Fourier infrared spectrum showed that the peak position of amide band I (1 600 similar to 1 700 cm(-1)) and amide band II (1 600 similar to 1 500 cm(-1)) of the RSA characteristic absorbing peaks was blueshifted. The amide band I moved from 1 650 to 1 710 cm(-1), and amide band II moved from 1 573 to 1 544 cm(-1), which indicated the structure of alpha helix features (1 650 similar to 1 658 cm(-1)) and beta-fold (1 620 similar to 1 640 cm(-1) and 1 645 cm(-1)) had changed The content of a-helical structure decreased from 42.15% to 1.27% by circular dichroism. The main reasons were the microenvironment polarity of tryptophan changed with the addition of CBBG-250 increased, two interaction between BSA and CBBG-250 including the hydrogen bonding and van der Waals force occurred, and then the secondary structure of BSA was changed, which was confirmed by Molecular modeling.
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