Study on the interaction between antibacterial drug and bovine serum albumin: a spectroscopic approach.

The binding of sulfamethoxazole (SMZ) to bovine serum albumin (BSA) was investigated by spectroscopic methods viz., fluorescence, FT-IR and UV-vis absorption techniques. The binding parameters have been evaluated by fluorescence quenching method. The thermodynamic parameters, Delta H degrees, DeltaS degrees and Delta G degrees were observed to be -58.0 kJ mol(-1), -111 J K(-1)mol(-1) and -24 kJ mol(-1), respectively. These indicated that the hydrogen bonding and weak van der Waals forces played a major role in the interaction. Based on the Forster's theory of non-radiation energy transfer, the binding average distance, r, between the donor (BSA) and acceptor (SMZ) was evaluated and found to be 4.12 nm. Spectral results showed the binding of SMZ to BSA induced conformational changes in BSA. The effect of common ions and some of the polymers used in drug delivery for control release was also tested on the binding of SMZ to BSA. The effect of common ions revealed that there is adverse effect on the binding of SMZ to BSA.