Studies on the Interaction of Cefepime Hydrochloride with Bovine Serum Albumin by Fluorescence, Synchronous Fluorescence, Three-Dimensional Fluorescence and Circular DichroismDaojin Li*
College of Chemistry and Chemical Engineering, Henan Key Laboratory of Function-Oriented Porous Materials, Luoyang Normal University, Luoyang, China
- *Corresponding Author:
- Daojin Li
College of Chemistry and Chemical Engineering
Henan Key Laboratory of Function-Oriented Porous Materials,
Luoyang Normal University, Luoyang, China
E-mail: [email protected]
Received Date: March 08, 2017; Accepted Date: April 11, 2017; Published Date: April 19, 2017
Citation: Li D (2017) Studies on the Interaction of Cefepime Hydrochloride with Bovine Serum Albumin by Fluorescence, Synchronous Fluorescence, Three- Dimensional Fluorescence and Circular Dichroism. J Bioanal Biomed 9:107-113. doi: 10.4172/1948-593X.1000162
Copyright: © 2017 Li D. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
The investigation on the binding mode between drug and protein is extremely important to understand biopharmaceutics, pharmacokinetics and toxicity of the drug as well as the relationship of structure and function of the protein. It is well proved that biological activity is a function of the chemical structure or structural properties. There is a study on the interaction of cefepime hydrochloride with serum albumin using in-silico molecular docking. But up to date, there is hardly any interaction investigation of cefepime hydrochloride with serum albumin utilizing by fluorescence, synchronous fluorescence, three-dimensional fluorescence and circular dichroism. In this study, the interaction of cefepime hydrochloride with bovine serum albumin in aqueous solution has been investigated by molecular spectroscopy under different pH conditions. The quenching rate constant and binding constant calculated at pH 7.4 indicated the static quenching mechanism and medium binding force. The effect of cefepime hydrochloride on the conformation of bovine serum albumin was analyzed using fluorescence, synchronous fluorescence, threedimensional fluorescence and circular dichroism. In addition, influence of pH on the binding of cefepime hydrochloride to bovine serum albumin was investigated and the binding ability of the drug to bovine serum albumin deceased under other pH conditions (pH 1.9, 3.5, and 9.0) as compared with that at pH 7.4. As compared with the binding ability of cefepime hydrochloride to native bovine serum albumin that of cefepime hydrochloride to denatured bovine serum albumin deceases dramatically. Furthermore, the effect of metal ions on the binding constant of cefepime hydrochloride with bovine serum albumin was investigated.