Investigation of the interaction between aspirin and bovine serum albumin using fluorescence spectroscopyAuthor(s): Baosheng Liu, Lihui Zhang, Zhiyun Li, Ying Guo
Under simulated physiological conditions (pH = 7.4), the reaction mechanism between aspirin and bovine serum albumin (BSA) at different temperatures (293K, 303 K, 310K)was investigated by the fluorescence spectroscopy (method 1) with focus on the fluorescence change of protein, as well as the fluorescence spectroscopy (method 2) with focus on the fluorescence change of drug. The results indicated that the electrostatic force played an important role on the conjugation reaction between aspirin and BSA. The binding constant obtained from method 2 was larger than the one obtained from method 1 by two orders of magnitude for the aspirin- BSA system. This indicated that the method 2 with focus on the fluorescence change of drug was a more accurate and more reasonable method. At last the correctness of method 2 was verified by UV-vis absorption spectroscopy and synchronous fluorescence spectroscopy with focus on the fluorescence change of drug.