目的利用荧光光谱法研究昂丹司琼(OND)与人血清白蛋白(HSA)的相互作用。方法采用荧光光谱法。结果在296K和310K时OND与HSA的结合常数分别为3.24×104L/mol,4.68×104L/mol,热力学参数ΔH为20.08kJ/mol。结论 OND对HSA的荧光猝灭机制主要为静态猝灭,二者有一个结合位点,其作用力类型以疏水作用力为主。% Objective Study on the interaetion for human serum albumin with ondansetron by Fluorescence Spectrometry. Methods Fluorescence spectrometry was used. Results The binding constants were 3.24×104 L/mol, 4.68×104 L/mol. The thermodynamic parametersΔH was 20.08kJ/mol. Conclusion The fluorescence quenching of HSA by OND indicated that the quenching mechanism was a static quenching, and the thermodynamic parameters showed that the interaction of OND and HSA was mainly driven by hydrophobic force.
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