Binding of naproxen and amitriptyline to bovine serum albumin: biophysical aspects

The Journal of Physical Chemistry. B
Tuhina BanerjeeNand Kishore

Abstract

Binding of the drugs naproxen (which is an anti-inflammatory) and amitriptyline (which is an anti-depressant) to bovine serum albumin (BSA) has been studied using isothermal titration calorimetry (ITC), in combination with fluorescence and circular dichroism spectroscopies. Naproxen is observed to bind more strongly to BSA than amitriptyline. The temperature-dependent ITC results indicate the interaction of one molecule of naproxen with more than one protein molecule. On the other hand, amitriptyline binds to BSA with a reaction stoichiometry that varies from 1:1.2 to 1:2.9. The van't Hoff enthalpy, which is calculated from the temperature dependence of the binding constant, agrees well with the calorimetric enthalpy in the case of naproxen binding to BSA, indicating adherence to a two-state binding process. However, their disagreement in the case of amitriptyline indicates conformational changes in the protein upon ligand binding, as well as with the rise in temperature. The spectroscopic results did not suggest appreciable conformational changes as a result of binding; hence, the discrepancy could be attributed to the temperature-induced conformational changes. With increases in the ionic strength, a reduction in the binding ...Continue Reading

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