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

Chundan Wang; Baosheng Liu; Lihua Ma; Hongcai Zhang; Xu Cheng

doi:doi:10.11648/j.jcebe.20180201.14

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

Chundan Wang, Baosheng Liu, Lihua Ma, Hongcai Zhang, Xu Cheng

Published in Journal of Chemical, Environmental and Biological Engineering (Volume 2, Issue 1)

Received: 4 May 2018 Accepted: 6 June 2018 Published: 4 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 (K_a) was 10⁴. The value of Hill’s coefficients (n_H) 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.

Published in	Journal of Chemical, Environmental and Biological Engineering (Volume 2, Issue 1)
DOI	10.11648/j.jcebe.20180201.14
Page(s)	17-25
Creative Commons	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), 2018. Published by Science Publishing Group

Keywords

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

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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://article.sciencepublishinggroup.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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Author Information

Chundan Wang

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

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

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

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

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

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Plain Text BibTeX RIS

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

Copy | Download

@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://article.sciencepublishinggroup.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}
}

Copy | Download

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  -

Copy | Download