The Investigation on the Interaction of Colistin Sulfate with Bovine Serum Albumin with Resonance Light Scattering Spectroscopy
ZHANG Qiu-ju, LIU Bao-sheng*, LI Gai-xia, HAN Rong, Lü Yun-kai
Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding 071002, China
Abstract：The interaction between colistin sulfate (CS) with bovine serum albumin in physiological buffer (pH 7.4) was investigated with resonance light scattering spectroscopy at 298, 310, and 318 K. The analysis of data indicated that quenching mechanism of BSA-CS was probably static. The value of n was approximately 1, indicating there was only a single class of binding sites on BSA for CS compounds. The thermodynamic parameters were calculated at different temperatures, implying that the interaction was spontaneous and electrostatic force played major role in the binding between CS and BSA. The values of nH were equal to 1 at different temperatures, indicating there was non-cooperative reaction between BSA and CS. The feasibility of resonance light scattering spectroscopy was verified by fluorescence quenching spectroscopy. The quenching reactive parameters (KSV，Kq，n，Ka) from two methods were similar, suggesting resonance light scattering spectroscopy could be used to study the binding interaction between protein and drugs. Resonance light scattering spectroscopy can be used to explore the substance without intrinsic fluorescence, suggesting that the application of resonance light scattering spectroscopy broadens the understanding of the interaction between small molecules and protein.
张秋菊，刘保生*，李改霞，韩 荣，吕运开 . 共振光散射法研究硫酸粘杆菌素与牛血清白蛋白间的反应机理 [J]. 光谱学与光谱分析, 2016, 36(09): 2879-2883.
ZHANG Qiu-ju, LIU Bao-sheng*, LI Gai-xia, HAN Rong, Lü Yun-kai . The Investigation on the Interaction of Colistin Sulfate with Bovine Serum Albumin with Resonance Light Scattering Spectroscopy . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2016, 36(09): 2879-2883.
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