Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods

Jinju Wang; Baosheng Liu; Shaotong Duan; Tongtong Li

doi:doi:10.11648/j.ajop.20170506.14

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Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods

Jinju Wang, Baosheng Liu, Shaotong Duan, Tongtong Li

Published in American Journal of Optics and Photonics (Volume 5, Issue 6)

Received: 10 January 2017 Accepted: 31 January 2017 Published: 12 January 2018

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Abstract

The binding of cefonicid sodium (CFS) with trypsin was investigated by spectroscopic and molecular docking methods under different temperatures conditions (303, 310 and 318 K). The results demonstrated that the interaction between CFS and trypsin was taking place via static quenching with 1:1 binding ratio. The fluorescence datas were treated by using the double logarithmic equation, and the binding constants K_a of the interaction of CFS-trypsin systems and the number of binding sites n were obtained. The thermodynamic parameters of CFS-trypsin systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them were mainly hydrophobic interaction and hydrogen bonding interaction, and with the molecular docking results are consistent.

Published in	American Journal of Optics and Photonics (Volume 5, Issue 6)
DOI	10.11648/j.ajop.20170506.14
Page(s)	80-87
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

Cefonicid Sodium, Trypsin, Spectrometry, Interaction, Molecular Docking

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APA Style

Jinju Wang, Baosheng Liu, Shaotong Duan, Tongtong Li. (2018). Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods. American Journal of Optics and Photonics, 5(6), 80-87. https://doi.org/10.11648/j.ajop.20170506.14

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ACS Style

Jinju Wang; Baosheng Liu; Shaotong Duan; Tongtong Li. Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods. Am. J. Opt. Photonics 2018, 5(6), 80-87. doi: 10.11648/j.ajop.20170506.14

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AMA Style

Jinju Wang, Baosheng Liu, Shaotong Duan, Tongtong Li. Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods. Am J Opt Photonics. 2018;5(6):80-87. doi: 10.11648/j.ajop.20170506.14

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@article{10.11648/j.ajop.20170506.14,
  author = {Jinju Wang and Baosheng Liu and Shaotong Duan and Tongtong Li},
  title = {Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods},
  journal = {American Journal of Optics and Photonics},
  volume = {5},
  number = {6},
  pages = {80-87},
  doi = {10.11648/j.ajop.20170506.14},
  url = {https://doi.org/10.11648/j.ajop.20170506.14},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajop.20170506.14},
  abstract = {The binding of cefonicid sodium (CFS) with trypsin was investigated by spectroscopic and molecular docking methods under different temperatures conditions (303, 310 and 318 K). The results demonstrated that the interaction between CFS and trypsin was taking place via static quenching with 1:1 binding ratio. The fluorescence datas were treated by using the double logarithmic equation, and the binding constants Ka of the interaction of CFS-trypsin systems and the number of binding sites n were obtained. The thermodynamic parameters of CFS-trypsin systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them were mainly hydrophobic interaction and hydrogen bonding interaction, and with the molecular docking results are consistent.},
 year = {2018}
}

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TY  - JOUR
T1  - Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods
AU  - Jinju Wang
AU  - Baosheng Liu
AU  - Shaotong Duan
AU  - Tongtong Li
Y1  - 2018/01/12
PY  - 2018
N1  - https://doi.org/10.11648/j.ajop.20170506.14
DO  - 10.11648/j.ajop.20170506.14
T2  - American Journal of Optics and Photonics
JF  - American Journal of Optics and Photonics
JO  - American Journal of Optics and Photonics
SP  - 80
EP  - 87
PB  - Science Publishing Group
SN  - 2330-8494
UR  - https://doi.org/10.11648/j.ajop.20170506.14
AB  - The binding of cefonicid sodium (CFS) with trypsin was investigated by spectroscopic and molecular docking methods under different temperatures conditions (303, 310 and 318 K). The results demonstrated that the interaction between CFS and trypsin was taking place via static quenching with 1:1 binding ratio. The fluorescence datas were treated by using the double logarithmic equation, and the binding constants Ka of the interaction of CFS-trypsin systems and the number of binding sites n were obtained. The thermodynamic parameters of CFS-trypsin systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them were mainly hydrophobic interaction and hydrogen bonding interaction, and with the molecular docking results are consistent.
VL  - 5
IS  - 6
ER  -

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Author Information

Jinju Wang

Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China
Baosheng Liu

Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China
Shaotong Duan

Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China
Tongtong Li

Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding, P. R. China

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Plain Text BibTeX RIS

APA Style

Jinju Wang, Baosheng Liu, Shaotong Duan, Tongtong Li. (2018). Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods. American Journal of Optics and Photonics, 5(6), 80-87. https://doi.org/10.11648/j.ajop.20170506.14

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ACS Style

Jinju Wang; Baosheng Liu; Shaotong Duan; Tongtong Li. Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods. Am. J. Opt. Photonics 2018, 5(6), 80-87. doi: 10.11648/j.ajop.20170506.14

Copy | Download

AMA Style

Jinju Wang, Baosheng Liu, Shaotong Duan, Tongtong Li. Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods. Am J Opt Photonics. 2018;5(6):80-87. doi: 10.11648/j.ajop.20170506.14

Copy | Download

@article{10.11648/j.ajop.20170506.14,
  author = {Jinju Wang and Baosheng Liu and Shaotong Duan and Tongtong Li},
  title = {Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods},
  journal = {American Journal of Optics and Photonics},
  volume = {5},
  number = {6},
  pages = {80-87},
  doi = {10.11648/j.ajop.20170506.14},
  url = {https://doi.org/10.11648/j.ajop.20170506.14},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajop.20170506.14},
  abstract = {The binding of cefonicid sodium (CFS) with trypsin was investigated by spectroscopic and molecular docking methods under different temperatures conditions (303, 310 and 318 K). The results demonstrated that the interaction between CFS and trypsin was taking place via static quenching with 1:1 binding ratio. The fluorescence datas were treated by using the double logarithmic equation, and the binding constants Ka of the interaction of CFS-trypsin systems and the number of binding sites n were obtained. The thermodynamic parameters of CFS-trypsin systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them were mainly hydrophobic interaction and hydrogen bonding interaction, and with the molecular docking results are consistent.},
 year = {2018}
}

Copy | Download

TY  - JOUR
T1  - Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods
AU  - Jinju Wang
AU  - Baosheng Liu
AU  - Shaotong Duan
AU  - Tongtong Li
Y1  - 2018/01/12
PY  - 2018
N1  - https://doi.org/10.11648/j.ajop.20170506.14
DO  - 10.11648/j.ajop.20170506.14
T2  - American Journal of Optics and Photonics
JF  - American Journal of Optics and Photonics
JO  - American Journal of Optics and Photonics
SP  - 80
EP  - 87
PB  - Science Publishing Group
SN  - 2330-8494
UR  - https://doi.org/10.11648/j.ajop.20170506.14
AB  - The binding of cefonicid sodium (CFS) with trypsin was investigated by spectroscopic and molecular docking methods under different temperatures conditions (303, 310 and 318 K). The results demonstrated that the interaction between CFS and trypsin was taking place via static quenching with 1:1 binding ratio. The fluorescence datas were treated by using the double logarithmic equation, and the binding constants Ka of the interaction of CFS-trypsin systems and the number of binding sites n were obtained. The thermodynamic parameters of CFS-trypsin systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them were mainly hydrophobic interaction and hydrogen bonding interaction, and with the molecular docking results are consistent.
VL  - 5
IS  - 6
ER  -

Copy | Download