Abstract
The binding of naproxen (NP) and 1-anilino-8-naphtalenesulphonic acid (ANS) to bovine serum albumin (BSA) has been studied by equilibrium dialysis and spectrophotofluorometry, respectively. The drug protein (D/P) ratio is found to determine the nature of binding sites for NP but not for ANS. At low D/P ratio, NP possesses a specific site in BSA and one of the tryptophan residues is part of it. Fluorometric investigation reveals non-displacement of ANS from its sites by the binding of NP to its specific site. At high D/P ratio, NP instead causes localized conformational changes in BSA. Furthermore, it is possible to infer the location of NP's specific site as loop 4 of BSA. NP and ANS binding sites have also been examined by employing Bromocresol Green (BCG) as a spectrophotometric probe. Competition studies are also able to establish distinct binding pattern for the two ligands in BSA. The displacement pattern points out the presence of independent sites for NP (specific site) and ANS (initially occupied site) in BSA in spite of their amphipathically similar nature.
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