The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin

Shaotong Duan; Baosheng Liu; Tongtong Li; Mengmeng Cui

doi:doi:10.11648/j.sjac.20160406.14

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The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin

Shaotong Duan, Baosheng Liu, Tongtong Li, Mengmeng Cui

Published in Science Journal of Analytical Chemistry (Volume 4, Issue 6)

Received: 12 September 2016 Accepted: 12 December 2016 Published: 8 January 2017

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Abstract

The interactions of cefoperazone sodium with bovine transferrin and bovine serum albumin were studied by multi-spectroscopic methods. Results showed that the intrinsic fluorescence of proteins was quenched by the cefoperazone sodium with a static quenching procedure. The thermodynamics parameters indicated that electrostatic attraction played a major role in the interactions of drug and proteins. The results of synchronous fluorescence spectra demonstrated that the microenvironments of amino acid residues of the two proteins were disturbed by cefoperazone sodium and the binding site of cefoperazone sodium to the bovine transferrin/bovine serum albumin was closer to tryptophan residues. Circular dichroism indicated that cefoperazone sodium changed the secondary structures of the two proteins. Hill’s coefficient showed that there was negative cooperation in the interaction of subsequent cefoperazone sodium with bovine transferrin/bovine serum albumin. Moreover, the results showed that cefoperazone sodium bound to bovine serum albumin with higher affinity. However, cefoperazone sodium had larger influences on the microenvironment of bovine transferrin. The interaction between cefoperazone sodium and different proteins will be helpful for extracting the common features, applying the unique characteristic of drug-proteins systems.

Published in	Science Journal of Analytical Chemistry (Volume 4, Issue 6)
DOI	10.11648/j.sjac.20160406.14
Page(s)	103-115
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), 2017. Published by Science Publishing Group

Keywords

Bovine Transferrin, Bovine Serum Albumin, Cefoperazone Sodium, Cooperativity, Multi-spectroscopic Methods

References

[1]	Firouzeh Manouchehri, Yahya Izadmanesh, Elham Aghaee, Jahan B. Ghasemi. Experimental, computational and chemometrics studies of BSA-vitamin B6 interaction by UV-Vis, FT-IR, fluorescence spectroscopy, molecular dynamics simulation and hard-soft modeling methods, Bioorg Chem. 2016; 68: 124-136.
[2]	Jie-hua Shi, Dong-qi Pan, Xiou-xiou Wang, et al. Characterizing the binding interaction between antimalarial artemether (AMT) and bovine serum albumin (BSA): Spectroscopic and molecular docking methods. J Photoch Photobio B. 2016; 162: 14-23.
[3]	Sun ZZ, Xu HD, Cao Y, Wang F, Mi WD. Elucidating the interaction of propofol and serum albumin by spectroscopic and docking methods. J Mol Liq. 2016; 219: 405-410.
[4]	Lin JJ, Liu Y, Chen MM, Huang HY, Song L. Investigation on the binding activities of citalopram with human and bovine serum albumins. J Lumin. 2014; 146: 114-122.
[5]	Attia T, El-Komy A, El-Hewaity M, Latif AAE, El-Hanbally S. Comparative pharmacokinetics of cefoperazone following intravenous and intramuscular administration in goats. International Journal of Veterinary Science and Medicine. 2015; 3 (1-2): 21-25.
[6]	Yuan YS, Fu SH, Xu QY, Yang JD, Hu XL, Liu SP. The fluorescence and resonance Rayleigh scattering spectral study and analytical application of cerium (IV) and cefoperazone system. Spectrochim Acta A. 2016; 162: 93-97.
[7]	Mehtab S, Gonçalves G, Roy S, et al. Interaction of vanadium (IV) with human serum apo-transferrin. J Inorg Biochem. 2013; 121: 187-195.
[8]	Moghaddam MM, Pirouzi M, Saberib MR, Chamani, J. Comparison of the binding behavior of FCCP with HSA and HTF as determined by spectroscopic and molecular modeling techniques. Luminescence. 2014; 29: 314-331.
[9]	Chamani JK, Vahedian-Movahed H, Saberi MR. Lomefloxacin promotes the interaction between human serum albumin and transferrin: A mechanistic insight into the emergence of antibiotic’s side effects. J pharmaceut biomed. 2011; 55: 114-124.
[10]	Zhang XF, Han RM, Sun XR, et al. The effect of the skeleton structure of flavanone and flavonoid on interaction with transferrin. Bioorg med chem lett. 2013, 23, 6677-6681.
[11]	Singh RP, Sharma G. Transferrin receptor targeted PLA-TPGS micelles improved efficacy and safety in docetaxel delivery. Int. J. Biol. Macromol. 2016, 83, 335-344.
[12]	Luck AN, Mason AB. Structure and dynamics of drug carriers and their interaction with cellular receptors: Focus on serum transferrin. Adv Drug Deliver Rev. 2013; 65: 1012-1019.
[13]	Ren HY, Xin X, Wang L, Ju HF. A direct comparison of the interaction of bovine serum albumin and gelatin with sodium deoxycholate in aqueous solutions. J Mol Liq. 2015; 207: 164-170.
[14]	Yan J, Wang Q, Pan QQ, et al. Assessment of the interaction between fraxinellone and bovine serum albumin by optical spectroscopy and molecular modeling methods. J Lumin. 2013; 137: 180-185.
[15]	Veerappan A, Eichhorn T, Zeino M, et al. Differential interactions of the broad spectrum drugs artemisinin, dihydroartemisinin and artesunate with serum albumin. Phytomedicine. 2013; 20: 969-974.
[16]	Yu XY, Yang Y, Liu RH, et al. The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches. J Lumin. 2011; 131: 1510-1514.
[17]	Yang J, Jing ZH, Jie JJ, Guo P. Fluorescence spectroscopy study on the interaction between Gossypol and bovine serum albumin. J. Mol. Struct. 2009; 920: 227.
[18]	Gou M, Fan WX, Wu RH. Interaction of Magnolol with HSA /BSA and Analysis of the Feasibility of Modeling Equation. Chin Pharm J. 2013; 48 (24): 2089-2097.
[19]	Xu HL, Yao N, Li GY, Li ZQ. Spectroscopic Studies on the Interaction Between Aucubin and Bovine Serum Albumin Without or With Copper II or Iron III. Spectrosc Lett. 2014; 47: 119-130.
[20]	Yu XY, Yang Y, Zou X, et al. Study on the interaction between novel spiro pyrrolidine and bovine serum albumin by spectroscopic techniques. Spectrochim Acta A. 2012; 94: 23-29.
[21]	Wang RY, Wang XG, Li ZG, et al. Study on the interaction between bovine serum albumin and 40-azido-20-deoxyfluoroarabinocytidine or analogs by spectroscopy and molecular modeling. Spectrochim Acta A. 2014; 132: 786-794.
[22]	Liu JW, Wang QY, Zhang H, et al. Interaction of chlorogenic acid with milk proteins analyzed by spectroscopic and modeling methods, Spectrosc Lett. 2016; 49 (1): 44-50.
[23]	Wang YP, Zhang GW, Wang LD. Interaction of prometryn to human serum albumin: Insights from spectroscopic and molecular docking studies. Pestic Biochem Phys. 2014; 108: 66-73.
[24]	Deng FY, Dong CY, Liu Y, Yu YM. Study on the Interaction Between Trimethoprim and Human Serum Albumin by Spectroscopic and Molecular Modeling Methods. Spectrosc Lett. 2013; 46 (1): 13-20.
[25]	Zhang SL, Yao HK, Wang CY, Tam KY. Study the interactions between human serum albumin and two antifungal drugs: Fluconazole and its analogue DTP. Bioorg Med Chem Lett. 2014; 24: 4963-4968.
[26]	Li HL, Zhan LY, Zhuang SL, Ni CX, Shang HW. Fluorescence Investigation on the Interaction of a Prevalent Competitive Fluorescent Probe with Entomic Odorant Binding Protein. Spectrosc Lett. 2013, 46, 527-534.
[27]	Sudha N, Sameena Y, Chandrasekarasekaran S, et al. Alteration of the Binding Strength of Dronedarone with Bovine Serum Albumin by β-Cyclodextrin: A Spectroscopic Study. Spectrosc Lett. 2014, 48, 112-119.
[28]	Ghosh S, Jana S, Guchhait N. Domain Specific Association of Small Fluorescent Probe trans-3-(4-Monomethylaminophenyl)-Acrylonitrile (MMAPA) with Bovine Serum Albumin (bovine serum albumin) and Its Dissociation from Protein Binding Sites by Ag Nanoparticles: Spectroscopic and Molecular Docking Study. J Phys Chem B. 2012; 116 (3): 1155-1163.
[29]	Wang J, Guo YW, Liu B, et al. Spectroscopic analyses on interaction of bovine serum albumin (bovine serum albumin) with toluidine blue (TB) and its sonodynamic damage under ultrasonic irradiation. J Lumin. 2011, 131, 231-237.
[30]	Enyedy ÉA, Horváth L, Hetényi A, et al. Interactions of the carrier ligands of antidiabetic metal complexes with human serum albumin: A combined spectroscopic and separation approach with molecular modeling studies. Bioorg Med Chem Lett. 2011; 19: 4202-4210.
[31]	Maciazek-Jurczyk M, Sulkowska A, Bojko B, et al. Fluorescence analysis of competition of phenylbutazone and methotrexate in binding to serum albumin in combination treatment in rheumatology. J mol struct. 2009; 924-926: 378-384.
[32]	Huang L, Li LZ, Li HL, et al. Interaction Between NeuroglobinandCaffeine by Multispectroscopic Methods. Spectrosc Lett. 2013; 46: 433-440.
[33]	Hemmateenejad B, Shamsipur M, Samari F, et al. Combined fluorescence spectroscopy and molecular modeling studies on the interaction between harmalol and human serum albumin. J pharmaceut biomed. 2012; 67-68: 201-208.
[34]	Zhu SZ, Liu Y. Spectroscopic analyses on interaction of Naphazoline hydrochloride with bovine serum albumin. Spectrochim Acta A. 2012; 98: 142-147.
[35]	Chen DD, Wu Q, Wang J, Wang Q, Qiao H. Spectroscopic analyses and studies on respective interaction of cyanuric acid and uric acid with bovine serum albumin and melamine. Spectrochim Acta A. 2015; 135: 511-520.
[36]	Liang LX, Zhao WH, Meng FY, et al. Synthesis of Amide Compounds of Ferulic Acid and Their Association with Bovine Serum Albumin. Spectroscopy Letters 2013, 46, 544-553.
[37]	Zhu YL, Zhang RX, Wang YX, et al. Biophysical study on the interaction of an anesthetic, vecuronium bromide with human serum albumin using spectroscopic and calorimetric methods. J Photoch Photobio B. 2014; 140: 381-389.
[38]	Wei JT, Jin F, Wu Q, et al. Molecular interaction study of flavonoid derivative 3d with human serum albumin using multispectroscopic and molecular modeling approach. Talanta. 2014; 126: 116-121.
[39]	Jattinagoudar L, Meti M, Nandibewoor S, Chimatadar S. Evaluation of the binding interaction between bovine serum albumin and dimethyl fumarate, an anti-inflammatory drug by multispectroscopic methods. Spectrochim Acta A. 2016; 156: 164-171.
[40]	Zhang J, Yan QS, Liu JP, Lu XH, et al. Study of the interaction between 5-sulfosalicylic acid and bovine serum albumin by fluorescence spectroscopy. J Lumin. 2013; 134: 747-753.
[41]	Shi JH, Zhu YY, Wang J, Chen J, Shen YJ. Intermolecular interaction of prednisolone with bovine serum albumin: Spectroscopic and molecular docking methods. Spectrochim Acta A. 2013; 103: 287-294.
[42]	Naseri A, Hosseini S, Rasoulzadeh F, et al. Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches. J Lumin. 2015; 157: 104-112.
[43]	Bojko B, Sułkowska A, Maciazek-Jurczyk M, et al. The influence of dietary habits and pathological conditions on the binding of theophylline to serum albumin. J pharmaceut biomed. 2010; 52 (3): 384-390.
[44]	Han R, Liu BS, Li GX, Zhang QJ. Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy. Luminescence. 2016; 31 (2): 580-586.

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APA Style

Shaotong Duan, Baosheng Liu, Tongtong Li, Mengmeng Cui. (2017). The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin. Science Journal of Analytical Chemistry, 4(6), 103-115. https://doi.org/10.11648/j.sjac.20160406.14

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ACS Style

Shaotong Duan; Baosheng Liu; Tongtong Li; Mengmeng Cui. The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin. Sci. J. Anal. Chem. 2017, 4(6), 103-115. doi: 10.11648/j.sjac.20160406.14

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AMA Style

Shaotong Duan, Baosheng Liu, Tongtong Li, Mengmeng Cui. The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin. Sci J Anal Chem. 2017;4(6):103-115. doi: 10.11648/j.sjac.20160406.14

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@article{10.11648/j.sjac.20160406.14,
  author = {Shaotong Duan and Baosheng Liu and Tongtong Li and Mengmeng Cui},
  title = {The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin},
  journal = {Science Journal of Analytical Chemistry},
  volume = {4},
  number = {6},
  pages = {103-115},
  doi = {10.11648/j.sjac.20160406.14},
  url = {https://doi.org/10.11648/j.sjac.20160406.14},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.sjac.20160406.14},
  abstract = {The interactions of cefoperazone sodium with bovine transferrin and bovine serum albumin were studied by multi-spectroscopic methods. Results showed that the intrinsic fluorescence of proteins was quenched by the cefoperazone sodium with a static quenching procedure. The thermodynamics parameters indicated that electrostatic attraction played a major role in the interactions of drug and proteins. The results of synchronous fluorescence spectra demonstrated that the microenvironments of amino acid residues of the two proteins were disturbed by cefoperazone sodium and the binding site of cefoperazone sodium to the bovine transferrin/bovine serum albumin was closer to tryptophan residues. Circular dichroism indicated that cefoperazone sodium changed the secondary structures of the two proteins. Hill’s coefficient showed that there was negative cooperation in the interaction of subsequent cefoperazone sodium with bovine transferrin/bovine serum albumin. Moreover, the results showed that cefoperazone sodium bound to bovine serum albumin with higher affinity. However, cefoperazone sodium had larger influences on the microenvironment of bovine transferrin. The interaction between cefoperazone sodium and different proteins will be helpful for extracting the common features, applying the unique characteristic of drug-proteins systems.},
 year = {2017}
}

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TY  - JOUR
T1  - The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin
AU  - Shaotong Duan
AU  - Baosheng Liu
AU  - Tongtong Li
AU  - Mengmeng Cui
Y1  - 2017/01/08
PY  - 2017
N1  - https://doi.org/10.11648/j.sjac.20160406.14
DO  - 10.11648/j.sjac.20160406.14
T2  - Science Journal of Analytical Chemistry
JF  - Science Journal of Analytical Chemistry
JO  - Science Journal of Analytical Chemistry
SP  - 103
EP  - 115
PB  - Science Publishing Group
SN  - 2376-8053
UR  - https://doi.org/10.11648/j.sjac.20160406.14
AB  - The interactions of cefoperazone sodium with bovine transferrin and bovine serum albumin were studied by multi-spectroscopic methods. Results showed that the intrinsic fluorescence of proteins was quenched by the cefoperazone sodium with a static quenching procedure. The thermodynamics parameters indicated that electrostatic attraction played a major role in the interactions of drug and proteins. The results of synchronous fluorescence spectra demonstrated that the microenvironments of amino acid residues of the two proteins were disturbed by cefoperazone sodium and the binding site of cefoperazone sodium to the bovine transferrin/bovine serum albumin was closer to tryptophan residues. Circular dichroism indicated that cefoperazone sodium changed the secondary structures of the two proteins. Hill’s coefficient showed that there was negative cooperation in the interaction of subsequent cefoperazone sodium with bovine transferrin/bovine serum albumin. Moreover, the results showed that cefoperazone sodium bound to bovine serum albumin with higher affinity. However, cefoperazone sodium had larger influences on the microenvironment of bovine transferrin. The interaction between cefoperazone sodium and different proteins will be helpful for extracting the common features, applying the unique characteristic of drug-proteins systems.
VL  - 4
IS  - 6
ER  -

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Author Information

Shaotong Duan

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
Tongtong Li

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

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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APA Style

Shaotong Duan, Baosheng Liu, Tongtong Li, Mengmeng Cui. (2017). The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin. Science Journal of Analytical Chemistry, 4(6), 103-115. https://doi.org/10.11648/j.sjac.20160406.14

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ACS Style

Shaotong Duan; Baosheng Liu; Tongtong Li; Mengmeng Cui. The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin. Sci. J. Anal. Chem. 2017, 4(6), 103-115. doi: 10.11648/j.sjac.20160406.14

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AMA Style

Shaotong Duan, Baosheng Liu, Tongtong Li, Mengmeng Cui. The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin. Sci J Anal Chem. 2017;4(6):103-115. doi: 10.11648/j.sjac.20160406.14

Copy | Download

@article{10.11648/j.sjac.20160406.14,
  author = {Shaotong Duan and Baosheng Liu and Tongtong Li and Mengmeng Cui},
  title = {The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin},
  journal = {Science Journal of Analytical Chemistry},
  volume = {4},
  number = {6},
  pages = {103-115},
  doi = {10.11648/j.sjac.20160406.14},
  url = {https://doi.org/10.11648/j.sjac.20160406.14},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.sjac.20160406.14},
  abstract = {The interactions of cefoperazone sodium with bovine transferrin and bovine serum albumin were studied by multi-spectroscopic methods. Results showed that the intrinsic fluorescence of proteins was quenched by the cefoperazone sodium with a static quenching procedure. The thermodynamics parameters indicated that electrostatic attraction played a major role in the interactions of drug and proteins. The results of synchronous fluorescence spectra demonstrated that the microenvironments of amino acid residues of the two proteins were disturbed by cefoperazone sodium and the binding site of cefoperazone sodium to the bovine transferrin/bovine serum albumin was closer to tryptophan residues. Circular dichroism indicated that cefoperazone sodium changed the secondary structures of the two proteins. Hill’s coefficient showed that there was negative cooperation in the interaction of subsequent cefoperazone sodium with bovine transferrin/bovine serum albumin. Moreover, the results showed that cefoperazone sodium bound to bovine serum albumin with higher affinity. However, cefoperazone sodium had larger influences on the microenvironment of bovine transferrin. The interaction between cefoperazone sodium and different proteins will be helpful for extracting the common features, applying the unique characteristic of drug-proteins systems.},
 year = {2017}
}

Copy | Download

TY  - JOUR
T1  - The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin
AU  - Shaotong Duan
AU  - Baosheng Liu
AU  - Tongtong Li
AU  - Mengmeng Cui
Y1  - 2017/01/08
PY  - 2017
N1  - https://doi.org/10.11648/j.sjac.20160406.14
DO  - 10.11648/j.sjac.20160406.14
T2  - Science Journal of Analytical Chemistry
JF  - Science Journal of Analytical Chemistry
JO  - Science Journal of Analytical Chemistry
SP  - 103
EP  - 115
PB  - Science Publishing Group
SN  - 2376-8053
UR  - https://doi.org/10.11648/j.sjac.20160406.14
AB  - The interactions of cefoperazone sodium with bovine transferrin and bovine serum albumin were studied by multi-spectroscopic methods. Results showed that the intrinsic fluorescence of proteins was quenched by the cefoperazone sodium with a static quenching procedure. The thermodynamics parameters indicated that electrostatic attraction played a major role in the interactions of drug and proteins. The results of synchronous fluorescence spectra demonstrated that the microenvironments of amino acid residues of the two proteins were disturbed by cefoperazone sodium and the binding site of cefoperazone sodium to the bovine transferrin/bovine serum albumin was closer to tryptophan residues. Circular dichroism indicated that cefoperazone sodium changed the secondary structures of the two proteins. Hill’s coefficient showed that there was negative cooperation in the interaction of subsequent cefoperazone sodium with bovine transferrin/bovine serum albumin. Moreover, the results showed that cefoperazone sodium bound to bovine serum albumin with higher affinity. However, cefoperazone sodium had larger influences on the microenvironment of bovine transferrin. The interaction between cefoperazone sodium and different proteins will be helpful for extracting the common features, applying the unique characteristic of drug-proteins systems.
VL  - 4
IS  - 6
ER  -

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