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Calorimetric and spectroscopic studies on the interaction of methimazole with bovine serum albumin

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Title Calorimetric and spectroscopic studies on the interaction of methimazole with bovine serum albumin
 
Creator SINGH, SK
KISHORE, N
 
Subject drug binding-sites
protein denaturation
beta-lactoglobulin
mechanism
hyperthyroidism
complexation
stability
bovine serum albumin
methimazole
calorimetry (itc)
circular dichroism
fluorescence spectroscopy
uv-vis spectroscopy
thermal denaturation
surfactants
 
Description The potential binding interaction(s) of the anti-thyroid drug methimazole (MMZ) with the protein bovine serum albumin (BSA) has been studied using isothermal titration calorimetry (ITC) and UV-Visible, fluorescence and circular dichroism (CD) spectroscopic techniques. The binding of MMZ to BSA has been studied in both the presence and absence of added surfactants. Since, the ITC thermograms show the molar enthalpy of binding of MMZ and BSA to be zero within experimental error, either the enthalpy change of the binding interaction is zero or there is no binding occurring. The CD and the intrinsic fluorescence and life time spectra of BSA were unchanged by the addition of MMZ. This is also indicative of the absence of any significant interaction of MMZ with BSA. (C) 2007 Wiley-Liss, Inc. and the American Pharmacists Association.
 
Publisher JOHN WILEY & SONS INC
 
Date 2011-08-04T11:23:52Z
2011-12-26T12:54:41Z
2011-12-27T05:42:53Z
2011-08-04T11:23:52Z
2011-12-26T12:54:41Z
2011-12-27T05:42:53Z
2008
 
Type Article
 
Identifier JOURNAL OF PHARMACEUTICAL SCIENCES, 97(6), 2362-2372
0022-3549
http://dx.doi.org/10.1002/jps.21140
http://dspace.library.iitb.ac.in/xmlui/handle/10054/9343
http://hdl.handle.net/10054/9343
 
Language en