Journal of Chemical, Environmental and Biological Engineering

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Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method

Received: 04 May 2018    Accepted: 06 June 2018    Published: 04 July 2018
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Abstract

The reaction mechanism of rhodamine B (RHB) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy and synchronous fluorescence spectroscopy at different temperatures (298 K, 310 K and 318 K). The results showed that electrostatic force played a major role on the conjugation reaction between BSA and RHB, and the type of quenching was static quenching. Primary binding site for RHB was sub-hydrophobic domain IIA, and the number of binding sites was 1. The order of magnitude of binding constants (Ka) was 104. The value of Hill’s coefficients (nH) was approximately equal to 1, which suggested no cooperativity in BSA-RHB system. The donor-to-acceptor distance r < 7 nm indicated that the static fluorescence quenching of BSA by RHB was also a non-radiation energy transfer process. The results of two methods were consistent that showed the synchronous fluorescence spectroscopy could be used to study the reaction mechanism between drug and protein, and was a useful supplement to the conventional fluorescence quenching method.

DOI 10.11648/j.jcebe.20180201.14
Published in Journal of Chemical, Environmental and Biological Engineering (Volume 2, Issue 1, June 2018)
Page(s) 17-25
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This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Fluorescence Spectroscopy, Synchronous Fluorescence Spectroscopy, Rhodamine B, Bovine Serum Albumin, Reaction Mechanism

References
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Author Information
  • College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China

  • College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China

  • College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China

  • College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China

  • College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China

Cite This Article
  • APA Style

    Chundan Wang, Baosheng Liu, Lihua Ma, Hongcai Zhang, Xu Cheng. (2018). Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method. Journal of Chemical, Environmental and Biological Engineering, 2(1), 17-25. https://doi.org/10.11648/j.jcebe.20180201.14

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    ACS Style

    Chundan Wang; Baosheng Liu; Lihua Ma; Hongcai Zhang; Xu Cheng. Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method. J. Chem. Environ. Biol. Eng. 2018, 2(1), 17-25. doi: 10.11648/j.jcebe.20180201.14

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    AMA Style

    Chundan Wang, Baosheng Liu, Lihua Ma, Hongcai Zhang, Xu Cheng. Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method. J Chem Environ Biol Eng. 2018;2(1):17-25. doi: 10.11648/j.jcebe.20180201.14

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  • @article{10.11648/j.jcebe.20180201.14,
      author = {Chundan Wang and Baosheng Liu and Lihua Ma and Hongcai Zhang and Xu Cheng},
      title = {Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method},
      journal = {Journal of Chemical, Environmental and Biological Engineering},
      volume = {2},
      number = {1},
      pages = {17-25},
      doi = {10.11648/j.jcebe.20180201.14},
      url = {https://doi.org/10.11648/j.jcebe.20180201.14},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.jcebe.20180201.14},
      abstract = {The reaction mechanism of rhodamine B (RHB) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy and synchronous fluorescence spectroscopy at different temperatures (298 K, 310 K and 318 K). The results showed that electrostatic force played a major role on the conjugation reaction between BSA and RHB, and the type of quenching was static quenching. Primary binding site for RHB was sub-hydrophobic domain IIA, and the number of binding sites was 1. The order of magnitude of binding constants (Ka) was 104. The value of Hill’s coefficients (nH) was approximately equal to 1, which suggested no cooperativity in BSA-RHB system. The donor-to-acceptor distance r < 7 nm indicated that the static fluorescence quenching of BSA by RHB was also a non-radiation energy transfer process. The results of two methods were consistent that showed the synchronous fluorescence spectroscopy could be used to study the reaction mechanism between drug and protein, and was a useful supplement to the conventional fluorescence quenching method.},
     year = {2018}
    }
    

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  • TY  - JOUR
    T1  - Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method
    AU  - Chundan Wang
    AU  - Baosheng Liu
    AU  - Lihua Ma
    AU  - Hongcai Zhang
    AU  - Xu Cheng
    Y1  - 2018/07/04
    PY  - 2018
    N1  - https://doi.org/10.11648/j.jcebe.20180201.14
    DO  - 10.11648/j.jcebe.20180201.14
    T2  - Journal of Chemical, Environmental and Biological Engineering
    JF  - Journal of Chemical, Environmental and Biological Engineering
    JO  - Journal of Chemical, Environmental and Biological Engineering
    SP  - 17
    EP  - 25
    PB  - Science Publishing Group
    SN  - 2640-267X
    UR  - https://doi.org/10.11648/j.jcebe.20180201.14
    AB  - The reaction mechanism of rhodamine B (RHB) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy and synchronous fluorescence spectroscopy at different temperatures (298 K, 310 K and 318 K). The results showed that electrostatic force played a major role on the conjugation reaction between BSA and RHB, and the type of quenching was static quenching. Primary binding site for RHB was sub-hydrophobic domain IIA, and the number of binding sites was 1. The order of magnitude of binding constants (Ka) was 104. The value of Hill’s coefficients (nH) was approximately equal to 1, which suggested no cooperativity in BSA-RHB system. The donor-to-acceptor distance r < 7 nm indicated that the static fluorescence quenching of BSA by RHB was also a non-radiation energy transfer process. The results of two methods were consistent that showed the synchronous fluorescence spectroscopy could be used to study the reaction mechanism between drug and protein, and was a useful supplement to the conventional fluorescence quenching method.
    VL  - 2
    IS  - 1
    ER  - 

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