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Insights into the binding of the drugs diclofenac sodium and cefotaxime sodium to serum albumin: Calorimetry and spectroscopy

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Title Insights into the binding of the drugs diclofenac sodium and cefotaxime sodium to serum albumin: Calorimetry and spectroscopy
 
Creator SHARMA, R
CHOUDHARY, S
KISHORE, N
 
Subject Bovine serum albumin
Diclofenac
Cefotaxime
Calorimetry
Binding thermodynamics
Spectroscopy
IONIC SURFACTANTS
BOVINE BSA
SITES
CEPHALOSPORINS
FLUORESCENCE
COMPLEXES
SPECIFICITY
CONSTANTS
PROTEINS
PROBES
 
Description Understanding physical chemistry underlying drug-protein interactions is essential to devise guidelines for the synthesis of target oriented drugs. Binding of a non-steroidal anti-inflammatory drug, diclofenac sodium (DCF) and an antibiotic drug, cefotaxime sodium (CFT) belonging to the family of cephalosporins with bovine serum albumin (BSA) has been examined using a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady state and time resolved fluorescence and circular dichroism spectroscopies. Binding affinity of both DCF and CFT with BSA is observed to be of the order of 10(4) M-1, with the binding profiles fitting well to the single set of binding site model. The disagreement between calorimetric and van't Hoff enthalpies indicates non-adherence to a two-state binding process which could be attributed to changes in the conformation of the protein upon ligand binding as well as with increase in the temperature. Circular dichroism and the fluorescence results, however, do not show any major conformational changes upon binding of these drugs to BSA, and hence the discrepancy could be due to temperature induced conformational changes in the protein. The results of ionic strength dependence and binding in the presence of anionic, cationic and non-ionic surfactants indicate, involvement of more that a single type of interaction in the binding process. The ITC results for the binding of these drugs to BSA in presence of each other indicate that the binding sites for the two drugs are different, and therefore binding of one is not influenced by the other. The DSC results provide quantitative information on the effect of these drugs on the stability of serum albumin. The combined calorimetric and spectroscopic approach has provided a detailed analysis including thermodynamics of the binding of DCF and CFI' with BSA qualitatively and quantitatively. (C) 2012 Elsevier B.V. All rights reserved.
 
Publisher ELSEVIER SCIENCE BV
 
Date 2014-10-15T08:29:49Z
2014-10-15T08:29:49Z
2012
 
Type Article
 
Identifier EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES, 46(5)435-445
http://dx.doi.org/10.1016/j.ejps.2012.03.007
http://dspace.library.iitb.ac.in/jspui/handle/100/14686
 
Language en