Biophysical Study on the Interaction of Ceftriaxone Sodium with Bovine Serum Albumin Using Spectroscopic Methods
| Autor: | Zhuo Cao, Jiongwei Pan, Liangxing Wang, Xiaoping Cai, Zaiting Ye |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Circular dichroism
biology Ceftriaxone Sodium Chemistry Hydrogen bond Health Toxicology and Mutagenesis Serum albumin Analytical chemistry General Medicine Toxicology Biochemistry Binding constant Crystallography symbols.namesake Förster resonance energy transfer biology.protein symbols Molecular Medicine Bovine serum albumin van der Waals force Molecular Biology |
| Zdroj: | Journal of Biochemical and Molecular Toxicology. 26:487-492 |
| ISSN: | 1095-6670 |
| DOI: | 10.1002/jbt.21446 |
| Popis: | The interaction of ceftriaxone sodium (CS), a cephalosporin antibiotic, with the major transport protein, bovine serum albumin (BSA), was investigated using different spectroscopic techniques such as fluorescence, circular dichroism (CD), and UV–vis spectroscopy. Values of binding parameters for BSA–CS interaction in terms of binding constant and number of binding sides were found to be 9.00 × 103, 3.24 × 103, and 2.30 × 103 M−1 at 281, 301, and 321 K, respectively. Thermodynamic analysis of the binding data obtained at different temperatures showed that the binding process was spontaneous and was primarily mediated by van der Waals force or hydrogen bonding. CS binding to BSA caused secondary structural alterations in the protein as revealed by CD results. The distance between CS and Trp of BSA was determined as 3.23 nm according to the Forster resonance energy transfer theory. © 2012 Wiley Periodicals, Inc. J Biochem Mol Toxicol 26:487-492, 2012; View this article online at wileyonlinelibrary.com. DOI 10.1002/jbt.21446 |
| Databáze: | OpenAIRE |
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