The mechanism of the interaction between bovine serum albumin (BSA) and ceftriaxone was studied employing fluorescence, and circular dichroism (CD) spectral methods. The intrinsic fluorescence of BSA and HSA was quenched by ceftriaxone in a static quenching mode, which was authenticated by Stern-Volmercalculations. The binding constant was obtained, which indicated a spontaneous and hydrophobic interaction between ceftriaxone with BSA and ceftriaxone with HSA with ceftriaxone. The present work uses spectroscopy to elucidate the mechanism behind the interaction between BSA, HSA and ceftriaxone. The BSA and ceftriaxone complex provides a model for studying drug-protein interactions and thus may further facilitate the study of drug metabolism and transportation. The binding properties on ceftriaxone to human serum albumin (HSA) have been studied for the first time using fluorescence spectroscopy, and circular dichroism (CD) spectroscopy. The results of spectroscopic measurements suggested that the hydrophobic interaction is the predominant intermolecular force stabilizing the complex, which is in good agreement with the results of molecule modeling study.
