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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/9343

Title: Calorimetric and spectroscopic studies on the interaction of methimazole with bovine serum albumin
Authors: SINGH, SK
KISHORE, N
Keywords: drug binding-sites
protein denaturation
beta-lactoglobulin
mechanism
hyperthyroidism
complexation
stability
Issue Date: 2008
Publisher: JOHN WILEY & SONS INC
Citation: JOURNAL OF PHARMACEUTICAL SCIENCES, 97(6), 2362-2372
Abstract: 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.
URI: http://dx.doi.org/10.1002/jps.21140
http://dspace.library.iitb.ac.in/xmlui/handle/10054/9343
http://hdl.handle.net/10054/9343
ISSN: 0022-3549
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