Volume 4, Issue 6, November 2016, Page: 103-115
The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin
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
Received: Sep. 12, 2016;       Accepted: Dec. 12, 2016;       Published: Jan. 8, 2017
DOI: 10.11648/j.sjac.20160406.14      View  2893      Downloads  99
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.
Bovine Transferrin, Bovine Serum Albumin, Cefoperazone Sodium, Cooperativity, Multi-spectroscopic Methods
To cite this article
Shaotong Duan, Baosheng Liu, Tongtong Li, Mengmeng Cui, The Interaction of Cefoperazone Sodium with Bovine Transferrin and Bovine Serum Albumin, Science Journal of Analytical Chemistry. Vol. 4, No. 6, 2016, pp. 103-115. doi: 10.11648/j.sjac.20160406.14
Copyright © 2016 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.
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