Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy

Hongcai Zhang; Baosheng Liu; Xu Cheng; Jinju Wang

doi:doi:10.11648/j.jddmc.20180401.12

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Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy

Hongcai Zhang, Baosheng Liu, Xu Cheng, Jinju Wang

Published in Journal of Drug Design and Medicinal Chemistry (Volume 4, Issue 1)

Received: 4 May 2018 Accepted: 7 June 2018 Published: 28 June 2018

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Abstract

The binding mechanism between cefetamet pivoxil (CFP) and pepsin (PEP) at different temperatures (298 K, 303 K, 310 K) was investigated by the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the improved spectroscopy with focus on the fluorescence changes of the resonance light scattering of small molecule drugs. The results showed that the main quenching mode of PEP-CFP was static quenching. The value of n was approximately equal to 1 which indicating that there was only one binding site in the interaction between PEP and CFP and the Hill coefficient was about 1 which indicating that there was no cooperative between the receptor PEP and ligand CFP. The binding constants of the PEP-CFP system obtained by the improved spectroscopic method were two orders of magnitude larger than that of the traditional fluorescence spectroscopy, which showed that the study of the small drug molecule was more practical and reasonable. The rationality of the experimental results obtained was verified by ultraviolet absorption spectroscopy.

Published in	Journal of Drug Design and Medicinal Chemistry (Volume 4, Issue 1)
DOI	10.11648/j.jddmc.20180401.12
Page(s)	5-9
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), 2024. Published by Science Publishing Group

Keywords

Cefetamet Pivoxil, Pepsin, Fluorescence Method, Improved Spectroscopy, Mechanism of Action

References

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[12]	M He, Z Xia, Y Yin, et al. Chin. J. Mod. Appl. Pharm, 2004, 21, 429-432.
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APA Style

Hongcai Zhang, Baosheng Liu, Xu Cheng, Jinju Wang. (2018). Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy. Journal of Drug Design and Medicinal Chemistry, 4(1), 5-9. https://doi.org/10.11648/j.jddmc.20180401.12

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ACS Style

Hongcai Zhang; Baosheng Liu; Xu Cheng; Jinju Wang. Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy. J. Drug Des. Med. Chem. 2018, 4(1), 5-9. doi: 10.11648/j.jddmc.20180401.12

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AMA Style

Hongcai Zhang, Baosheng Liu, Xu Cheng, Jinju Wang. Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy. J Drug Des Med Chem. 2018;4(1):5-9. doi: 10.11648/j.jddmc.20180401.12

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@article{10.11648/j.jddmc.20180401.12,
  author = {Hongcai Zhang and Baosheng Liu and Xu Cheng and Jinju Wang},
  title = {Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy},
  journal = {Journal of Drug Design and Medicinal Chemistry},
  volume = {4},
  number = {1},
  pages = {5-9},
  doi = {10.11648/j.jddmc.20180401.12},
  url = {https://doi.org/10.11648/j.jddmc.20180401.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.jddmc.20180401.12},
  abstract = {The binding mechanism between cefetamet pivoxil (CFP) and pepsin (PEP) at different temperatures (298 K, 303 K, 310 K) was investigated by the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the improved spectroscopy with focus on the fluorescence changes of the resonance light scattering of small molecule drugs. The results showed that the main quenching mode of PEP-CFP was static quenching. The value of n was approximately equal to 1 which indicating that there was only one binding site in the interaction between PEP and CFP and the Hill coefficient was about 1 which indicating that there was no cooperative between the receptor PEP and ligand CFP. The binding constants of the PEP-CFP system obtained by the improved spectroscopic method were two orders of magnitude larger than that of the traditional fluorescence spectroscopy, which showed that the study of the small drug molecule was more practical and reasonable. The rationality of the experimental results obtained was verified by ultraviolet absorption spectroscopy.},
 year = {2018}
}

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TY  - JOUR
T1  - Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy
AU  - Hongcai Zhang
AU  - Baosheng Liu
AU  - Xu Cheng
AU  - Jinju Wang
Y1  - 2018/06/28
PY  - 2018
N1  - https://doi.org/10.11648/j.jddmc.20180401.12
DO  - 10.11648/j.jddmc.20180401.12
T2  - Journal of Drug Design and Medicinal Chemistry
JF  - Journal of Drug Design and Medicinal Chemistry
JO  - Journal of Drug Design and Medicinal Chemistry
SP  - 5
EP  - 9
PB  - Science Publishing Group
SN  - 2472-3576
UR  - https://doi.org/10.11648/j.jddmc.20180401.12
AB  - The binding mechanism between cefetamet pivoxil (CFP) and pepsin (PEP) at different temperatures (298 K, 303 K, 310 K) was investigated by the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the improved spectroscopy with focus on the fluorescence changes of the resonance light scattering of small molecule drugs. The results showed that the main quenching mode of PEP-CFP was static quenching. The value of n was approximately equal to 1 which indicating that there was only one binding site in the interaction between PEP and CFP and the Hill coefficient was about 1 which indicating that there was no cooperative between the receptor PEP and ligand CFP. The binding constants of the PEP-CFP system obtained by the improved spectroscopic method were two orders of magnitude larger than that of the traditional fluorescence spectroscopy, which showed that the study of the small drug molecule was more practical and reasonable. The rationality of the experimental results obtained was verified by ultraviolet absorption spectroscopy.
VL  - 4
IS  - 1
ER  -

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Author Information

Hongcai Zhang

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

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

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

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

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Plain Text BibTeX RIS

APA Style

Hongcai Zhang, Baosheng Liu, Xu Cheng, Jinju Wang. (2018). Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy. Journal of Drug Design and Medicinal Chemistry, 4(1), 5-9. https://doi.org/10.11648/j.jddmc.20180401.12

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ACS Style

Hongcai Zhang; Baosheng Liu; Xu Cheng; Jinju Wang. Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy. J. Drug Des. Med. Chem. 2018, 4(1), 5-9. doi: 10.11648/j.jddmc.20180401.12

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AMA Style

Hongcai Zhang, Baosheng Liu, Xu Cheng, Jinju Wang. Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy. J Drug Des Med Chem. 2018;4(1):5-9. doi: 10.11648/j.jddmc.20180401.12

Copy | Download

@article{10.11648/j.jddmc.20180401.12,
  author = {Hongcai Zhang and Baosheng Liu and Xu Cheng and Jinju Wang},
  title = {Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy},
  journal = {Journal of Drug Design and Medicinal Chemistry},
  volume = {4},
  number = {1},
  pages = {5-9},
  doi = {10.11648/j.jddmc.20180401.12},
  url = {https://doi.org/10.11648/j.jddmc.20180401.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.jddmc.20180401.12},
  abstract = {The binding mechanism between cefetamet pivoxil (CFP) and pepsin (PEP) at different temperatures (298 K, 303 K, 310 K) was investigated by the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the improved spectroscopy with focus on the fluorescence changes of the resonance light scattering of small molecule drugs. The results showed that the main quenching mode of PEP-CFP was static quenching. The value of n was approximately equal to 1 which indicating that there was only one binding site in the interaction between PEP and CFP and the Hill coefficient was about 1 which indicating that there was no cooperative between the receptor PEP and ligand CFP. The binding constants of the PEP-CFP system obtained by the improved spectroscopic method were two orders of magnitude larger than that of the traditional fluorescence spectroscopy, which showed that the study of the small drug molecule was more practical and reasonable. The rationality of the experimental results obtained was verified by ultraviolet absorption spectroscopy.},
 year = {2018}
}

Copy | Download

TY  - JOUR
T1  - Comparative Studies on the Interaction Between the Medicine Small Molecule with Pepsin by Fluorescence Quenching Spectroscopy and Improved Spectroscopy
AU  - Hongcai Zhang
AU  - Baosheng Liu
AU  - Xu Cheng
AU  - Jinju Wang
Y1  - 2018/06/28
PY  - 2018
N1  - https://doi.org/10.11648/j.jddmc.20180401.12
DO  - 10.11648/j.jddmc.20180401.12
T2  - Journal of Drug Design and Medicinal Chemistry
JF  - Journal of Drug Design and Medicinal Chemistry
JO  - Journal of Drug Design and Medicinal Chemistry
SP  - 5
EP  - 9
PB  - Science Publishing Group
SN  - 2472-3576
UR  - https://doi.org/10.11648/j.jddmc.20180401.12
AB  - The binding mechanism between cefetamet pivoxil (CFP) and pepsin (PEP) at different temperatures (298 K, 303 K, 310 K) was investigated by the classical fluorescence spectroscopy with focus on the fluorescence change of protein, as well as the improved spectroscopy with focus on the fluorescence changes of the resonance light scattering of small molecule drugs. The results showed that the main quenching mode of PEP-CFP was static quenching. The value of n was approximately equal to 1 which indicating that there was only one binding site in the interaction between PEP and CFP and the Hill coefficient was about 1 which indicating that there was no cooperative between the receptor PEP and ligand CFP. The binding constants of the PEP-CFP system obtained by the improved spectroscopic method were two orders of magnitude larger than that of the traditional fluorescence spectroscopy, which showed that the study of the small drug molecule was more practical and reasonable. The rationality of the experimental results obtained was verified by ultraviolet absorption spectroscopy.
VL  - 4
IS  - 1
ER  -

Copy | Download