光谱学与光谱分析 |
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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 |
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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.
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Received: 2015-06-09
Accepted: 2015-10-25
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Corresponding Authors:
LIU Bao-sheng
E-mail: lbs@hbu.edu.cn
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