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Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies

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Title Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies
 
Creator KESWANI, N
CHOUDHARY, S
KISHORE, N
 
Subject Bovine serum albumin
Oxytetracycline
Binding thermodynamics
Isothermal titration calorimetry
Differential scanning calorimetry
Spectroscopy
BINDING-SITES
IN-VITRO
LIGAND-BINDING
FATTY-ACIDS
PROTEIN
TETRACYCLINE
STABILITY
SUCROSE
SALT
STABILIZATION
 
Description A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (Delta H), entropy (Delta S), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 . 10(4) at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic interactions with a minor hydrogen bonding contribution in the drug-protein complexation. The DSC results on the binding of oxytetracycline with bovine serum albumin in the absence and presence of these additives provide quantitative information on the effect of drugs on the stability of bovine serum albumin, and suggest preferential complexation of one of the domains of the protein. The results further indicate that the drug occupies binding site II on bovine serum albumin. (C) 2012 Elsevier Ltd. All rights reserved.
 
Publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
 
Date 2014-10-16T06:44:09Z
2014-10-16T06:44:09Z
2013
 
Type Article
 
Identifier JOURNAL OF CHEMICAL THERMODYNAMICS, 58196-205
http://dx.doi.org/10.1016/j.jct.2012.11.006
http://dspace.library.iitb.ac.in/jspui/handle/100/15465
 
Language en