Abstract：In the Tris-HCl buffer solution with pH was 7.40, the interaction between glipizide (Gli) and bovine serum albumin (BSA) was investigated by classical fluorescence spectroscopy with the change of protein as investigation object and elastic scattering fluorescence spectrometry with the change of drugs as investigation object at 293 K and 303 K, the conclusions of the two methods were consistent. Results showed that Gli could quench the intrinsic fluorescence of BSA, and the quenching mechanism was a dynamic quenching process. The hydrophobic force played an important role in the conjugation reaction between BSA and Gli, the binding site mainly located in BSA hydrophobic region and the number of binding site (n) in the binary system was approximately to 1. The values of Hill’s coefficients were less than 1, which indicated the weak negative cooperativity in BSA-Gli system. The binding constant (Ka) obtained by elastic scattering fluorescence spectrometric was much larger than the one obtained by classical fluorescence spectroscopy, indiciating that it was more accurate and reasonable when using the change of drug’s fluorescence as the research object. At last, the scientificalness of the new method based on elastic scattering fluorescence spectrometric was verified by ultraviolet spectroscopy. The research results showed that there existed insufficiency in analysis of the interaction of drug with protein by classical fluorescence spectroscopy with the change of protein as investigation object, and the fluorescence spectrogram only reflected partial information of the interaction between drug and protein, while the interaction between drug and protein could be better expressed by elastic scattering fluorescence spectrometry with the change of drugs as investigation object.
刘保生，曹世娜，李志云，种宝红 . 格列吡嗪与牛血清白蛋白相互作用的分子光谱法的改进实验 [J]. 光谱学与光谱分析, 2014, 34(03): 762-766.
LIU Bao-sheng, CAO Shi-na, LI Zhi-yun, CHONG Bao-hong . Modification on the Interaction of Glipizide with Bovine Serum Albumin by Molecular Spectroscopy. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2014, 34(03): 762-766.
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