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
Volume 2, Issue 1, June 2018, Pages: 17-25
Received: May 4, 2018; Accepted: Jun. 6, 2018; Published: Jul. 4, 2018
Views 678      Downloads 59
Authors
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
Article Tools
Follow on us
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.
Keywords
Fluorescence Spectroscopy, Synchronous Fluorescence Spectroscopy, Rhodamine B, Bovine Serum Albumin, Reaction Mechanism
To cite this article
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, Journal of Chemical, Environmental and Biological Engineering. Vol. 2, No. 1, 2018, pp. 17-25. doi: 10.11648/j.jcebe.20180201.14
Copyright
Copyright © 2018 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
References
[1]
S. Millan, L. Satish, and S. Kesh, J. Photoch. Photobio., 2016, 162, 248-257.
[2]
Z. L. Yang, S. Chen, and Y. X. Zhao, Sensor. Actuat. B-Chem., 2018, 266, 422-428.
[3]
J. Ji, Y. Liu, and X. Y. Yang, J. Environ. Manage., 2018, 218, 300-308.
[4]
X. R. Li, Y. B. Hao, J. Mol. Struct., 2015, 1091, 109-117.
[5]
S. T. Duan, B. S. Liu, and T. T. Li, J. Appl. Spectrosc+., 2017, 84, 411-418.
[6]
G. X. Li, B. S. Liu, and Q. J. Zhang, Lumin., 2016, 31, 1054-1062.
[7]
P. Zhao, G. Gao, and L. J. Zhang, J. Pharmaceut. Biome., 2017, 141, 262-269.
[8]
F. A. Qais, I. Ahmad, J. Pharmaceut. Biome., 2018, 149, 193-205.
[9]
G. Rabbani, M. H. Baig, and A. T. Jan, Int. J. Biol. Macromol., 2017, 105, 1572-1580.
[10]
Z. J. Li, Z. C. Wang, and N. Wang, J. Pharmaceut. Biome., 2018, 149, 290-295.
[11]
A. Kaur, I. A. Khan, and P. K. Banipal, Spectrochim. Acta. A., 2018, 191, 259-270.
[12]
Z. Y. Tian, F. L. Zang, and W. Luo, J. Photochem. Photobiol. B., 2015, 142, 103-109.
[13]
J. E. Ali, P. A. Vahid, Food Chem., B. 2016, 202, 426-431.
[14]
Z. B. Wu, L. L. Shen, and J. Lu, Food Biophys., 2017, 12, 78-87.
[15]
M. K. Amroabadi, A. Taheri-Kafrani, and L. H. Saremi, Int. J. Biol. Macromol., 2018, 108, 263-271.
[16]
H. L. Xu, N. N. Yao, and G. Y. Li, Spectrosc. Lett., 2014, 47, 119-130.
[17]
S. N. Cao, B. S. Liu, and G. X. Li, J. Lumin., 2014, 145, 94-99.
[18]
M. Makarska-Bialokoz, Spectrochim. Acta. A., 2016, 193, 23-32.
[19]
G. X. Li, B. S. Liu, and Q. J. Zhang, Lumin., 2016, 31, 1054-1062.
[20]
C. B. Xu, J. L. Gu, and X. P. Ma, Spectrochim. Acta. A., 2014, 125, 391-395.
[21]
S. Huang, H. Qiu, and Y. Liu, Colloid. Surface. B, 2016, 148, 165-172.
[22]
M. B. Bolattin, S. T. Nandibewoor, and S. D. Joshi, Ind. Eng. Chem. Res., 2016, 55, 5454-5464.
[23]
Q. J. Zhang, B. S. Liu, and R. Han, Spectrosc. Lett., 2016, 49, 208-213.
[24]
A. Hasanzadeh, G. Dehghan, and M. Shaghaghi, J. Mol. Liq., 2017, 248, 459-467.
[25]
Z. G. Li, J. Q. Wang, and T. Ren, Med. Chem. Res., 2016, 25, 1009-1019.
[26]
A. T. Buddanavar, S. T. Nandibewoor, J. Pharmaceut Anal., 2017, 7, 148-155.
[27]
F. Moeinpour, F. S. Mohseni-Shahri, and B. Malaekeh-Nikouei, Chem-Biol. Interact., 2016, 257, 4-13.
ADDRESS
Science Publishing Group
1 Rockefeller Plaza,
10th and 11th Floors,
New York, NY 10020
U.S.A.
Tel: (001)347-983-5186